메뉴 건너뛰기




Volumn 9, Issue 1, 2014, Pages 75-91

Staphylococci: Colonizers and pathogens of human skin

Author keywords

adhesin; antimicrobial peptide; commensal; desiccation; fatty acid; pathogen; skin colonization; sphingosine; Staphylococcus

Indexed keywords

ADENOSINE PHOSPHATE; ADHESIN; ARGININE; COLLAGEN TYPE 1; CYTOKERATIN 10; FIBRINOGEN; FIBRONECTIN; GLYCOLIPID; INVOLUCRIN; LORICRIN; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEINASE; RIBONUCLEASE; RIBONUCLEASE 5; RIBONUCLEASE 7; RIBONUCLEASE A; SPHINGOSINE; UNCLASSIFIED DRUG;

EID: 84890580030     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.13.145     Document Type: Review
Times cited : (123)

References (164)
  • 1
    • 39049154328 scopus 로고    scopus 로고
    • Skin microbiota: A source of disease or defence?
    • Cogen A, Nizet V, Gallo R. Skin microbiota: A source of disease or defence?. Br. J. Dermatol. 158(3), 442-455 (2008).
    • (2008) Br. J Dermatol. , vol.158 , Issue.3 , pp. 442-455
    • Cogen, A.1    Nizet, V.2    Gallo, R.3
  • 2
    • 84868710891 scopus 로고    scopus 로고
    • Microbiome dynamics of human epidermis following skin barrier disruption
    • Zeeuwen P, Boekhorst J, van den Bogaard E et al. Microbiome dynamics of human epidermis following skin barrier disruption. Genome Biol. 13(11), R101 (2012).
    • (2012) Genome Biol. , vol.13 , Issue.11
    • Zeeuwen, P.1    Boekhorst, J.2    Van Den Bogaard, E.3
  • 3
    • 66349083859 scopus 로고    scopus 로고
    • Topographical and temporal diversity of the human skin microbiome
    • Grice E, Kong H, Conlan S et al. Topographical and temporal diversity of the human skin microbiome. Science 324(5931), 1190-1192 (2009).
    • (2009) Science , vol.324 , Issue.5931 , pp. 1190-1192
    • Grice, E.1    Kong, H.2    Conlan, S.3
  • 4
    • 33847305053 scopus 로고    scopus 로고
    • Molecular analysis of human forearm superficial skin bacterial biota
    • Gao Z, Tseng C, Pei Z, Blaser M. Molecular analysis of human forearm superficial skin bacterial biota. Proc. Natl Acad. Sci. USA 104(8), 2927-2932 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.8 , pp. 2927-2932
    • Gao, Z.1    Tseng, C.2    Pei, Z.3    Blaser, M.4
  • 6
    • 72949091232 scopus 로고    scopus 로고
    • Bacterial community variation in human body habitats across space and time
    • Costello E, Lauber C, Hamady M, Fierer N, Gordon J, Knight R. Bacterial community variation in human body habitats across space and time. Science 326(5960), 1694-1697 (2009).
    • (2009) Science , vol.326 , Issue.5960 , pp. 1694-1697
    • Costello, E.1    Lauber, C.2    Hamady, M.3    Fierer, N.4    Gordon, J.5    Knight, R.6
  • 7
    • 80052851309 scopus 로고    scopus 로고
    • Diversity of the human skin microbiome early in life
    • Capone K, Dowd S, Stamatas G, Nikolovski J. Diversity of the human skin microbiome early in life. J. Invest. Dermatol. 131(10), 2026-2032 (2011).
    • (2011) J. Invest. Dermatol. , vol.131 , Issue.10 , pp. 2026-2032
    • Capone, K.1    Dowd, S.2    Stamatas, G.3    Nikolovski, J.4
  • 8
    • 0014495767 scopus 로고
    • Normal flora of skin in different age groups
    • Somerville D. Normal flora of skin in different age groups. Br. J. Dermatol. 81(4), 248-258 (1969).
    • (1969) Br. J. Dermatol. , vol.81 , Issue.4 , pp. 248-258
    • Somerville, D.1
  • 9
    • 84867220740 scopus 로고    scopus 로고
    • Shifts in human skin and nares microbiota of healthy children and adults
    • Oh J, Conlan S, Polley E, Segre J, Kong H. Shifts in human skin and nares microbiota of healthy children and adults. Genome Med. 4(10), 77 (2012).
    • (2012) Genome Med. , vol.4 , Issue.10 , pp. 77
    • Oh, J.1    Conlan, S.2    Polley, E.3    Segre, J.4    Kong, H.5
  • 11
    • 17844393627 scopus 로고    scopus 로고
    • Nasal carriage of Staphylococcus aureus and prevention of nosocomial infections
    • Kluytmans J, Wertheim H. Nasal carriage of Staphylococcus aureus and prevention of nosocomial infections. Infection 33(1), 3-8 (2005).
    • (2005) Infection , vol.33 , Issue.1 , pp. 3-8
    • Kluytmans, J.1    Wertheim, H.2
  • 12
    • 0002984304 scopus 로고
    • Nose and skin carriage of Staphylococcus aureus in patients receiving penicillin
    • Moss B, Squire J. Nose and skin carriage of Staphylococcus aureus in patients receiving penicillin. Lancet 1(6496), 320-325 (1948).
    • (1948) Lancet , vol.1 , Issue.6496 , pp. 320-325
    • Moss, B.1    Squire, J.2
  • 13
    • 84876763587 scopus 로고    scopus 로고
    • Comparative epidemiology of Staphylococcus epidermidis isolates from patients with catheter-related bacteremia and from healthy volunteers
    • Cherifi S, Byl B, Deplano A, Nonhoff C, Denis O, Hallin M. Comparative epidemiology of Staphylococcus epidermidis isolates from patients with catheter-related bacteremia and from healthy volunteers. J. Clin. Microbiol. 51(5), 1541-1547 (2013).
    • (2013) J. Clin. Microbiol. , vol.51 , Issue.5 , pp. 1541-1547
    • Cherifi, S.1    Byl, B.2    Deplano, A.3    Nonhoff, C.4    Denis, O.5    Hallin, M.6
  • 14
    • 78149431872 scopus 로고    scopus 로고
    • Lucky number seven: RNase 7 can prevent Staphylococcus aureus skin colonization
    • Cho J, Xuan C, Miller L. Lucky number seven: RNase 7 can prevent Staphylococcus aureus skin colonization. J. Invest. Dermatol. 130(12), 2703-2706 (2010).
    • (2010) J. Invest. Dermatol. , vol.130 , Issue.12 , pp. 2703-2706
    • Cho, J.1    Xuan, C.2    Miller, L.3
  • 16
    • 33745518413 scopus 로고    scopus 로고
    • Epidermal differentiation complex yields a secret: Mutations in the cornification protein filaggrin underlie ichthyosis vulgaris
    • Segre J. Epidermal differentiation complex yields a secret: Mutations in the cornification protein filaggrin underlie ichthyosis vulgaris. J. Invest. Dermatol. 126(6), 1202-1204 (2006).
    • (2006) J. Invest. Dermatol. , vol.126 , Issue.6 , pp. 1202-1204
    • Segre, J.1
  • 17
    • 60749125436 scopus 로고    scopus 로고
    • Epidermal homeostasis: A balancing act of stem cells in the skin
    • Blanpain C, Fuchs E. Epidermal homeostasis: A balancing act of stem cells in the skin. Nat. Rev. Mol. Cell Biol. 10(3), 207-217 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , Issue.3 , pp. 207-217
    • Blanpain, C.1    Fuchs, E.2
  • 18
    • 80052382533 scopus 로고    scopus 로고
    • Corneodesmosomes and corneodesmosin: From the stratum corneum cohesion to the pathophysiology of genodermatoses
    • Jonca N, Leclerc E, Caubet C, Simon M, Guerrin M, Serre G. Corneodesmosomes and corneodesmosin: From the stratum corneum cohesion to the pathophysiology of genodermatoses. Eur. J. Dermatol. 21, 35-42 (2011).
    • (2011) Eur. J. Dermatol. , vol.21 , pp. 35-42
    • Jonca, N.1    Leclerc, E.2    Caubet, C.3    Simon, M.4    Guerrin, M.5    Serre, G.6
  • 19
    • 0017370855 scopus 로고
    • Cornified envelope of terminally differentiated human epidermal keratinocytes consists of cross-linked protein
    • Rice R, Green H. Cornified envelope of terminally differentiated human epidermal keratinocytes consists of cross-linked protein. Cell 11(2), 417-422 (1977).
    • (1977) Cell , vol.11 , Issue.2 , pp. 417-422
    • Rice, R.1    Green, H.2
  • 20
    • 0025941838 scopus 로고
    • Structure and function of lamellar bodies, lipid-protein complexes involved in storage and secretion of cellular lipids
    • Schmitz G, Müller G. Structure and function of lamellar bodies, lipid-protein complexes involved in storage and secretion of cellular lipids. J. Lipid Res. 32(10), 1539-1570 (1991).
    • (1991) J. Lipid Res. , vol.32 , Issue.10 , pp. 1539-1570
    • Schmitz, G.1    Müller, G.2
  • 21
    • 17144371855 scopus 로고    scopus 로고
    • The cornified envelope: A model of cell death in the skin
    • Candi E, Schmidt R, Melino G. The cornified envelope: A model of cell death in the skin. Nat. Rev. Mol. Cell Biol. 6(4), 328-340 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , Issue.4 , pp. 328-340
    • Candi, E.1    Schmidt, R.2    Melino, G.3
  • 22
    • 84863872233 scopus 로고    scopus 로고
    • Cell-extracellular matrix interactions in normal and diseased skin
    • doi:10.1101/cshperspect.a005124
    • Watt F, Fujiwara H. Cell-extracellular matrix interactions in normal and diseased skin. Cold Spring Harb. Perspect. Biol. 3(4), doi:10.1101/cshperspect. a005124 (2011).
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , Issue.4
    • Watt, F.1    Fujiwara, H.2
  • 23
    • 84865314766 scopus 로고    scopus 로고
    • The human skin barrier is organized as stacked bilayers of fully extended ceramides with cholesterol molecules associated with the ceramide sphingoid moiety
    • Iwai I, Han H, den Hollander L et al. The human skin barrier is organized as stacked bilayers of fully extended ceramides with cholesterol molecules associated with the ceramide sphingoid moiety. J. Invest. Dermatol. 132(9), 2215-2225 (2012).
    • (2012) J. Invest. Dermatol. , vol.132 , Issue.9 , pp. 2215-2225
    • Iwai, I.1    Han, H.2    Den Hollander, L.3
  • 24
    • 46449124442 scopus 로고    scopus 로고
    • A diversity profile of the human skin microbiota
    • Grice E, Kong H, Renaud G et al. A diversity profile of the human skin microbiota. Genome Res. 18(7), 1043-1050 (2008).
    • (2008) Genome Res. , vol.18 , Issue.7 , pp. 1043-1050
    • Grice, E.1    Kong, H.2    Renaud, G.3
  • 25
    • 77950920890 scopus 로고    scopus 로고
    • Temporal expression of adhesion factors and activity of global regulators during establishment of Staphylococcus aureus nasal colonization
    • Burian M, Rautenberg M, Kohler T et al. Temporal expression of adhesion factors and activity of global regulators during establishment of Staphylococcus aureus nasal colonization. J. Infect. Dis. 201(9), 1414-1421 (2010).
    • (2010) J. Infect. Dis. , vol.201 , Issue.9 , pp. 1414-1421
    • Burian, M.1    Rautenberg, M.2    Kohler, T.3
  • 26
    • 77956327503 scopus 로고    scopus 로고
    • Regulatory adaptation of Staphylococcus aureus during nasal colonization of humans
    • Burian M, Wolz C, Goerke C. Regulatory adaptation of Staphylococcus aureus during nasal colonization of humans. PLoS ONE 5(3), e10040 (2010).
    • (2010) PLoS ONE , vol.5 , Issue.3
    • Burian, M.1    Wolz, C.2    Goerke, C.3
  • 27
    • 2342639647 scopus 로고    scopus 로고
    • Role of teichoic acids in Staphylococcus aureus nasal colonization, a major risk factor in nosocomial infections
    • Weidenmaier C, Kokai-Kun J, Kristian S et al. Role of teichoic acids in Staphylococcus aureus nasal colonization, a major risk factor in nosocomial infections. Nat. Med. 10(3), 243-245 (2004).
    • (2004) Nat. Med. , vol.10 , Issue.3 , pp. 243-245
    • Weidenmaier, C.1    Kokai-Kun, J.2    Kristian, S.3
  • 28
    • 44449099612 scopus 로고    scopus 로고
    • Differential roles of sortase-Anchored surface proteins and wall teichoic acid in Staphylococcus aureus nasal colonization
    • Weidenmaier C, Kokai-Kun J, Kulauzovic E et al. Differential roles of sortase-Anchored surface proteins and wall teichoic acid in Staphylococcus aureus nasal colonization. Int. J. Med. Microbiol. 298(5-6), 505-513 (2008).
    • (2008) Int. J. Med. Microbiol. , vol.298 , Issue.5-6 , pp. 505-513
    • Weidenmaier, C.1    Kokai-Kun, J.2    Kulauzovic, E.3
  • 30
    • 54249096108 scopus 로고    scopus 로고
    • Pathogenomics of the staphylococci: Insights into niche adaptation and the emergence of new virulent strains
    • Ben Zakour N, Guinane C, Fitzgerald J. Pathogenomics of the staphylococci: Insights into niche adaptation and the emergence of new virulent strains. FEMS Microbiol. Lett. 289(1), 1-12 (2008).
    • (2008) FEMS Microbiol. Lett. , vol.289 , Issue.1 , pp. 1-12
    • Ben Zakour, N.1    Guinane, C.2    Fitzgerald, J.3
  • 31
    • 0142011077 scopus 로고    scopus 로고
    • The Staphylococcus aureus surface protein SasG and its homologues promote bacterial adherence to human desquamated nasal epithelial cells
    • Roche F, Meehan M, Foster T. The Staphylococcus aureus surface protein SasG and its homologues promote bacterial adherence to human desquamated nasal epithelial cells. Microbiology SGM 149, 2759-2767 (2003).
    • (2003) Microbiology SGM , vol.149 , pp. 2759-2767
    • Roche, F.1    Meehan, M.2    Foster, T.3
  • 32
    • 70350447804 scopus 로고    scopus 로고
    • The terminal A domain of the fibrillar accumulation-Associated protein (Aap) of Staphylococcus epidermidis mediates adhesion to human corneocytes
    • Macintosh R, Brittan J, Bhattacharya R et al. The terminal A domain of the fibrillar accumulation-Associated protein (Aap) of Staphylococcus epidermidis mediates adhesion to human corneocytes. J. Bacteriol. 191(22), 7007-7016 (2009).
    • (2009) J. Bacteriol. , vol.191 , Issue.22 , pp. 7007-7016
    • Macintosh, R.1    Brittan, J.2    Bhattacharya, R.3
  • 33
    • 0021151784 scopus 로고
    • The adhesion of coagulase negative staphylococci to human skin and its relevance to the bacterial flora of milk
    • Brooker B, Fuller R. The adhesion of coagulase negative staphylococci to human skin and its relevance to the bacterial flora of milk. J. Appl. Bacteriol. 57(2), 325-332 (1984).
    • (1984) J. Appl. Bacteriol. , vol.57 , Issue.2 , pp. 325-332
    • Brooker, B.1    Fuller, R.2
  • 34
    • 44949164634 scopus 로고    scopus 로고
    • Immunohistological study of involucrin expression in Darier's disease skin
    • Kassar S, Charfeddine C, Zribi H et al. Immunohistological study of involucrin expression in Darier's disease skin. J. Cutan. Pathol. 35(7), 635-640 (2008).
    • (2008) J. Cutan. Pathol. , vol.35 , Issue.7 , pp. 635-640
    • Kassar, S.1    Charfeddine, C.2    Zribi, H.3
  • 35
    • 37549031717 scopus 로고    scopus 로고
    • Reduced in vitro adherence of Staphylococcus species to feline corneocytes compared with canine and human corneocytes
    • Woolley K, Kelly R, Fazakerley J, Williams N, Nuttall T, McEwan N. Reduced in vitro adherence of Staphylococcus species to feline corneocytes compared with canine and human corneocytes. Vet. Dermatol. 19(1), 1-6 (2008).
    • (2008) Vet. Dermatol. , vol.19 , Issue.1 , pp. 1-6
    • Woolley, K.1    Kelly, R.2    Fazakerley, J.3    Williams, N.4    Nuttall, T.5    McEwan, N.6
  • 36
    • 33644830761 scopus 로고    scopus 로고
    • Adherence by Staphylococcus intermedius to canine corneocytes: A preliminary study comparing noninflamed and inflamed atopic canine skin
    • McEwan N, Mellor D, Kalna G. Adherence by Staphylococcus intermedius to canine corneocytes: A preliminary study comparing noninflamed and inflamed atopic canine skin. Vet. Dermatol. 17(2), 151-154 (2006).
    • (2006) Vet. Dermatol. , vol.17 , Issue.2 , pp. 151-154
    • McEwan, N.1    Mellor, D.2    Kalna, G.3
  • 37
    • 0034909507 scopus 로고    scopus 로고
    • Fibronectin and fibrinogen contribute to the enhanced binding of Staphylococcus aureus to atopic skin
    • Cho S, Strickland I, Boguniewicz M, Leung DY. Fibronectin and fibrinogen contribute to the enhanced binding of Staphylococcus aureus to atopic skin. J. Allergy Clin. Immunol. 108(2), 269-274 (2001).
    • (2001) J. Allergy Clin. Immunol. , vol.108 , Issue.2 , pp. 269-274
    • Cho, S.1    Strickland, I.2    Boguniewicz, M.3    Leung, D.Y.4
  • 38
    • 77951092674 scopus 로고    scopus 로고
    • Kallikrein expression and cathelicidin processing are independently controlled in keratinocytes by calcium, vitamin D-3, and retinoic acid
    • Morizane S, Yamasaki K, Kabigting F, Gallo R. Kallikrein expression and cathelicidin processing are independently controlled in keratinocytes by calcium, vitamin D-3, and retinoic acid. J. Invest. Dermatol. 130(5), 1297-1306 (2010).
    • (2010) J. Invest. Dermatol. , vol.130 , Issue.5 , pp. 1297-1306
    • Morizane, S.1    Yamasaki, K.2    Kabigting, F.3    Gallo, R.4
  • 39
    • 0034946112 scopus 로고    scopus 로고
    • Expression of the peptide antibiotics human beta defensin-1 and human beta defensin-2 in normal human skin
    • Ali R, Falconer A, Ikram M, Bisset C, Cerio R, Quinn A. Expression of the peptide antibiotics human beta defensin-1 and human beta defensin-2 in normal human skin. J. Invest. Dermatol. 117(1), 106-111 (2001).
    • (2001) J. Invest. Dermatol. , vol.117 , Issue.1 , pp. 106-111
    • Ali, R.1    Falconer, A.2    Ikram, M.3    Bisset, C.4    Cerio, R.5    Quinn, A.6
  • 40
    • 0036450262 scopus 로고    scopus 로고
    • Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin
    • Murakami M, Ohtake T, Dorschner R, Schittek B, Garbe C, Gallo R. Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin. J. Invest. Dermatol. 119(5), 1090-1095 (2002).
    • (2002) J. Invest. Dermatol. , vol.119 , Issue.5 , pp. 1090-1095
    • Murakami, M.1    Ohtake, T.2    Dorschner, R.3    Schittek, B.4    Garbe, C.5    Gallo, R.6
  • 41
    • 20444384801 scopus 로고    scopus 로고
    • Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo
    • Rieg S, Steffen H, Seeber S et al. Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo. J. Immunol. 174, 8003-8010 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 8003-8010
    • Rieg, S.1    Steffen, H.2    Seeber, S.3
  • 42
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz T. Defensins: Antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 3(9), 710-720 (2003).
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 43
    • 67049107846 scopus 로고    scopus 로고
    • Dermcidin-derived peptides show a different mode of action than the cathelicidin LL37 against Staphylococcus aureus
    • Senyurek I, Paulmann M, Sinnberg T et al. Dermcidin-derived peptides show a different mode of action than the cathelicidin LL37 against Staphylococcus aureus. Antimicrob. Agents Chemother. 53(6), 2499-2509 (2009).
    • (2009) Antimicrob. Agents Chemother. , vol.53 , Issue.6 , pp. 2499-2509
    • Senyurek, I.1    Paulmann, M.2    Sinnberg, T.3
  • 44
    • 84858054251 scopus 로고    scopus 로고
    • Structure-Activity analysis of the dermcidin-derived peptide DCD1L, an anionic antimicrobial peptide present in human sweat
    • Paulmann M, Arnold T, Linke D et al. Structure-Activity analysis of the dermcidin-derived peptide DCD1L, an anionic antimicrobial peptide present in human sweat. J. Biol. Chem. 287(11), 8434-8443 (2012).
    • (2012) J. Biol. Chem. , vol.287 , Issue.11 , pp. 8434-8443
    • Paulmann, M.1    Arnold, T.2    Linke, D.3
  • 45
    • 84875272220 scopus 로고    scopus 로고
    • Crystal structure and functional mechanism of a human antimicrobial membrane channel
    • Song C, Weichbrodt C, Salnikov E et al. Crystal structure and functional mechanism of a human antimicrobial membrane channel. PNAS 110(12), 4586-4591 (2013).
    • (2013) PNAS , vol.110 , Issue.12 , pp. 4586-4591
    • Song, C.1    Weichbrodt, C.2    Salnikov, E.3
  • 46
    • 0023004103 scopus 로고
    • De nevo synthesis of lysozyme by human epidermal cells
    • Chen V, France D, Martinelli G. De nevo synthesis of lysozyme by human epidermal cells. J. Invest. Dermatol. 87(5), 585-587 (1986).
    • (1986) J. Invest. Dermatol. , vol.87 , Issue.5 , pp. 585-587
    • Chen, V.1    France, D.2    Martinelli, G.3
  • 47
    • 13444282403 scopus 로고    scopus 로고
    • Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-Acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus
    • Bera A, Herbert S, Jakob A, Vollmer W, Gotz F. Why are pathogenic staphylococci so lysozyme resistant?. The peptidoglycan O-Acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol. Microbiol. 55(3), 778-787 (2005).
    • (2005) Mol. Microbiol. , vol.55 , Issue.3 , pp. 778-787
    • Bera, A.1    Herbert, S.2    Jakob, A.3    Vollmer, W.4    Gotz, F.5
  • 48
    • 34547629994 scopus 로고    scopus 로고
    • Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci
    • Herbert S, Bera A, Nerz C et al. Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci. PLoS Pathog. 3(7), 981-994 (2007).
    • (2007) PLoS Pathog. , vol.3 , Issue.7 , pp. 981-994
    • Herbert, S.1    Bera, A.2    Nerz, C.3
  • 49
    • 84872374733 scopus 로고    scopus 로고
    • The mammalian secreted RNases: Mechanisms of action in host defence
    • Gupta S, Haigh B, Griffin F, Wheeler T. The mammalian secreted RNases: Mechanisms of action in host defence. Innate Immunol. 19(1), 86-97 (2013).
    • (2013) Innate Immunol. , vol.19 , Issue.1 , pp. 86-97
    • Gupta, S.1    Haigh, B.2    Griffin, F.3    Wheeler, T.4
  • 50
    • 78149469147 scopus 로고    scopus 로고
    • RNase 7 protects healthy skin from Staphylococcus aureus colonization
    • Simanski M, Dressel S, Glaeser R, Harder J. RNase 7 protects healthy skin from Staphylococcus aureus colonization. J. Invest. Dermatol. 130(12), 2836-2838 (2010).
    • (2010) J. Invest. Dermatol. , vol.130 , Issue.12 , pp. 2836-2838
    • Simanski, M.1    Dressel, S.2    Glaeser, R.3    Harder, J.4
  • 51
    • 0037195896 scopus 로고    scopus 로고
    • RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin
    • Harder J, Schroder J. RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin. J. Biol. Chem. 277(48), 46779-46784 (2002).
    • (2002) J. Biol. Chem. , vol.277 , Issue.48 , pp. 46779-46784
    • Harder, J.1    Schroder, J.2
  • 52
    • 0037340434 scopus 로고    scopus 로고
    • Angiogenins: A new class of microbicidal proteins involved in innate immunity
    • Hooper L, Stappenbeck T, Hong C, Gordon J. Angiogenins: A new class of microbicidal proteins involved in innate immunity. Nat. Immunol. 4(3), 269-273 (2003).
    • (2003) Nat. Immunol. , vol.4 , Issue.3 , pp. 269-273
    • Hooper, L.1    Stappenbeck, T.2    Hong, C.3    Gordon, J.4
  • 53
    • 12844257490 scopus 로고    scopus 로고
    • The ribonuclease A superfamily of mammals and birds: Identifying new members and tracing evolutionary histories
    • Cho S, Beintema J, Zhang J. The ribonuclease A superfamily of mammals and birds: Identifying new members and tracing evolutionary histories. Genomics 85(2), 208-220 (2005).
    • (2005) Genomics , vol.85 , Issue.2 , pp. 208-220
    • Cho, S.1    Beintema, J.2    Zhang, J.3
  • 55
    • 70349745535 scopus 로고    scopus 로고
    • Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7
    • Abtin A, Eckhart L, Mildner M et al. Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7. J. Invest. Dermatol. 129(9), 2193-2201 (2009).
    • (2009) J. Invest. Dermatol. , vol.129 , Issue.9 , pp. 2193-2201
    • Abtin, A.1    Eckhart, L.2    Mildner, M.3
  • 56
    • 0034831403 scopus 로고    scopus 로고
    • Topically applied lactic acid increases spontaneous secretion of vascular endothelial growth factor by human reconstructed epidermis
    • Rendl M, Mayer C, Weninger W, Tschachler E. Topically applied lactic acid increases spontaneous secretion of vascular endothelial growth factor by human reconstructed epidermis. Br. J. Dermatol. 145(1), 3-9 (2001).
    • (2001) Br. J. Dermatol. , vol.145 , Issue.1 , pp. 3-9
    • Rendl, M.1    Mayer, C.2    Weninger, W.3    Tschachler, E.4
  • 57
    • 71949105323 scopus 로고    scopus 로고
    • Constitutive expression of the antimicrobial peptide RNase 7 is associated with Staphylococcus aureus infection of the skin
    • Zanger P, Holzer J, Schleucher R, Steffen H, Schittek B, Gabrysch S. Constitutive expression of the antimicrobial peptide RNase 7 is associated with Staphylococcus aureus infection of the skin. J. Infect. Dis. 200(12), 1907-1915 (2009).
    • (2009) J. Infect. Dis. , vol.200 , Issue.12 , pp. 1907-1915
    • Zanger, P.1    Holzer, J.2    Schleucher, R.3    Steffen, H.4    Schittek, B.5    Gabrysch, S.6
  • 58
    • 0037440095 scopus 로고    scopus 로고
    • Human RNase 7: A new cationic ribonuclease of the RNase A superfamily
    • Zhang J, Dyer K, Rosenberg H. Human RNase 7: A new cationic ribonuclease of the RNase A superfamily. Nucleic Acids Res. 31(2), 602-607 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , Issue.2 , pp. 602-607
    • Zhang, J.1    Dyer, K.2    Rosenberg, H.3
  • 59
    • 33947513637 scopus 로고    scopus 로고
    • The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity
    • Huang Y, Lin Y, Chang T et al. The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity. J. Biol. Chem. 282(7), 4626-4633 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.7 , pp. 4626-4633
    • Huang, Y.1    Lin, Y.2    Chang, T.3
  • 61
    • 79958166236 scopus 로고    scopus 로고
    • Growth-phase dependence of susceptibility to antimicrobial peptides in Staphylococcus aureus
    • Matsuo M, Oogai Y, Kato F, Sugai M, Komatsuzawa H. Growth-phase dependence of susceptibility to antimicrobial peptides in Staphylococcus aureus. Microbiology-SGM 157, 1786-1797 (2011).
    • (2011) Microbiology-SGM , vol.157 , pp. 1786-1797
    • Matsuo, M.1    Oogai, Y.2    Kato, F.3    Sugai, M.4    Komatsuzawa, H.5
  • 62
    • 36148999436 scopus 로고    scopus 로고
    • The antimicrobial peptide-sensing system aps of Staphylococcus aureus
    • Li M, Cha D, Lai Y, Villaruz A, Sturdevant D, Otto M. The antimicrobial peptide-sensing system aps of Staphylococcus aureus. Mol. Microbiol. 66(5), 1136-1147 (2007).
    • (2007) Mol. Microbiol. , vol.66 , Issue.5 , pp. 1136-1147
    • Li, M.1    Cha, D.2    Lai, Y.3    Villaruz, A.4    Sturdevant, D.5    Otto, M.6
  • 63
    • 34547622874 scopus 로고    scopus 로고
    • Interaction of the GraRS two-component system with the VraFG ABC transporter to support vancomycin-intermediate resistance in Staphylococcus aureus
    • Meehl M, Herbert S, Gotz F, Cheung A. Interaction of the GraRS two-component system with the VraFG ABC transporter to support vancomycin-intermediate resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 51(8), 2679-2689 (2007).
    • (2007) Antimicrob. Agents Chemother. , vol.51 , Issue.8 , pp. 2679-2689
    • Meehl, M.1    Herbert, S.2    Gotz, F.3    Cheung, A.4
  • 64
    • 84856069886 scopus 로고    scopus 로고
    • GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus
    • Falord M, Karimova G, Hiron A, Msadek T. GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 56(2), 1047-1058 (2012).
    • (2012) Antimicrob. Agents Chemother. , vol.56 , Issue.2 , pp. 1047-1058
    • Falord, M.1    Karimova, G.2    Hiron, A.3    Msadek, T.4
  • 65
    • 84863230616 scopus 로고    scopus 로고
    • The Staphylococcus aureus two-component regulatory system, GraRS, senses and confers resistance to selected cationic antimicrobial peptides
    • Yang S, Bayer A, Mishra N et al. The Staphylococcus aureus two-component regulatory system, GraRS, senses and confers resistance to selected cationic antimicrobial peptides. Infect. Immun. 80(1), 74-81 (2012).
    • (2012) Infect. Immun. , vol.80 , Issue.1 , pp. 74-81
    • Yang, S.1    Bayer, A.2    Mishra, N.3
  • 66
    • 1642555530 scopus 로고    scopus 로고
    • Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol
    • Oku Y, Kurokawa K, Ichihashi N, Sekimizu K. Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol. Microbiology-SGM 150, 45-51 (2004).
    • (2004) Microbiology-SGM , vol.150 , pp. 45-51
    • Oku, Y.1    Kurokawa, K.2    Ichihashi, N.3    Sekimizu, K.4
  • 67
    • 0842325226 scopus 로고    scopus 로고
    • MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance
    • Staubitz P, Neumann H, Schneider T, Wiedemann I, Peschel A. MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance. FEMS Microbiol. Lett. 231(1), 67-71 (2004).
    • (2004) FEMS Microbiol. Lett. , vol.231 , Issue.1 , pp. 67-71
    • Staubitz, P.1    Neumann, H.2    Schneider, T.3    Wiedemann, I.4    Peschel, A.5
  • 68
    • 0035821289 scopus 로고    scopus 로고
    • Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with L-lysine
    • Peschel A, Jack R, Otto M et al. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with L-lysine. J. Exp. Med. 193(9), 1067-1076 (2001).
    • (2001) J. Exp. Med. , vol.193 , Issue.9 , pp. 1067-1076
    • Peschel, A.1    Jack, R.2    Otto, M.3
  • 69
    • 79956318149 scopus 로고    scopus 로고
    • Multiple peptide resistance factor (MprF)-mediated resistance of Staphylococcus aureus against antimicrobial peptides coincides with a modulated peptide interaction with artificial membranes comprising lysyl- phosphatidylglycerol
    • Andrae J, Goldmann T, Ernst C, Peschel A, Gutsmann T. Multiple peptide resistance factor (MprF)-mediated resistance of Staphylococcus aureus against antimicrobial peptides coincides with a modulated peptide interaction with artificial membranes comprising lysyl-phosphatidylglycerol. J. Biol. Chem. 286(21), 18692-18700 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.21 , pp. 18692-18700
    • Andrae, J.1    Goldmann, T.2    Ernst, C.3    Peschel, A.4    Gutsmann, T.5
  • 70
    • 0028982844 scopus 로고
    • Incorporation of d-Alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis - identification of genes and regulation
    • Perego M, Glaser P, Minutello A, Strauch M, Leopold K, Fischer W. Incorporation of d-Alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis - identification of genes and regulation. J. Biol. Chem. 270(26), 15598-15606 (1995).
    • (1995) J. Biol. Chem. , vol.270 , Issue.26 , pp. 15598-15606
    • Perego, M.1    Glaser, P.2    Minutello, A.3    Strauch, M.4    Leopold, K.5    Fischer, W.6
  • 71
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel A, Otto M, Jack R, Kalbacher H, Jung G, Gotz F. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274(13), 8405-8410 (1999).
    • (1999) J. Biol. Chem. , vol.274 , Issue.13 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.3    Kalbacher, H.4    Jung, G.5    Gotz, F.6
  • 72
    • 33846079739 scopus 로고    scopus 로고
    • The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci
    • Lai Y, Villaruz A, Li M, Cha D, Sturdevant D, Otto M. The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci. Mol. Microbiol. 63(2), 497-506 (2007).
    • (2007) Mol. Microbiol. , vol.63 , Issue.2 , pp. 497-506
    • Lai, Y.1    Villaruz, A.2    Li, M.3    Cha, D.4    Sturdevant, D.5    Otto, M.6
  • 73
    • 39049169762 scopus 로고    scopus 로고
    • A potential new pathway for Staphylococcus aureus dissemination: The silent survival of S aureus phagocytosed by human monocyte-derived macrophages
    • Kubica M, Guzik K, Koziel J et al. A potential new pathway for Staphylococcus aureus dissemination: The silent survival of S. aureus phagocytosed by human monocyte-derived macrophages. PLoS ONE 3(1), e1409 (2008).
    • (2008) PLoS ONE , vol.3 , Issue.1
    • Kubica, M.1    Guzik, K.2    Koziel, J.3
  • 74
    • 60349085142 scopus 로고    scopus 로고
    • Staphylococcus aureus: New evidence for intracellular persistence
    • Garzoni C, Kelley W. Staphylococcus aureus: New evidence for intracellular persistence. Trends Microbiol. 17(2), 59-65 (2009).
    • (2009) Trends Microbiol. , vol.17 , Issue.2 , pp. 59-65
    • Garzoni, C.1    Kelley, W.2
  • 75
    • 79958050684 scopus 로고    scopus 로고
    • Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion
    • Laarman A, Ruyken M, Malone C, van Strijp J, Horswill A, Rooijakkers S. Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion. J. Immunol. 186(11), 6445-6453 (2011).
    • (2011) J. Immunol. , vol.186 , Issue.11 , pp. 6445-6453
    • Laarman, A.1    Ruyken, M.2    Malone, C.3    Van Strijp, J.4    Horswill, A.5    Rooijakkers, S.6
  • 76
    • 79953314786 scopus 로고    scopus 로고
    • Regulatory mechanism for exfoliative toxin production in Staphylococcus aureus
    • Kato F, Kadomoto N, Iwamoto Y, Bunai K, Komatsuzawa H, Sugai M. Regulatory mechanism for exfoliative toxin production in Staphylococcus aureus. Infect. Immun. 79(4), 1660-1670 (2011).
    • (2011) Infect. Immun. , vol.79 , Issue.4 , pp. 1660-1670
    • Kato, F.1    Kadomoto, N.2    Iwamoto, Y.3    Bunai, K.4    Komatsuzawa, H.5    Sugai, M.6
  • 77
    • 38149018614 scopus 로고    scopus 로고
    • Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli
    • Nemoto T, Ohara-Nemoto Y, Ono T et al. Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli. FEBS J. 275(3), 573-587 (2008).
    • (2008) FEBS J. , vol.275 , Issue.3 , pp. 573-587
    • Nemoto, T.1    Ohara-Nemoto, Y.2    Ono, T.3
  • 78
    • 75549085674 scopus 로고    scopus 로고
    • Staphylococcus aureus extracellular protease causes epidermal barrier dysfunction
    • Hirasawa Y, Takai T, Nakamura T et al. Staphylococcus aureus extracellular protease causes epidermal barrier dysfunction. J. Invest. Dermatol. 130(2), 614-617 (2010).
    • (2010) J. Invest. Dermatol. , vol.130 , Issue.2 , pp. 614-617
    • Hirasawa, Y.1    Takai, T.2    Nakamura, T.3
  • 79
    • 84890764250 scopus 로고    scopus 로고
    • Protease-Armed bacteria in the skin
    • Koziel J, Potempa J. Protease-Armed bacteria in the skin. Cell Tissue Res. 351(2), 325-337 (2013).
    • (2013) Cell Tissue Res. , vol.351 , Issue.2 , pp. 325-337
    • Koziel, J.1    Potempa, J.2
  • 80
    • 84874738695 scopus 로고    scopus 로고
    • Beta-hemolysin promotes skin colonization by Staphylococcus aureus
    • Katayama Y, Baba T, Sekine M, Fukuda M, Hiramatsu K. Beta-hemolysin promotes skin colonization by Staphylococcus aureus. J. Bacteriol. 195(6), 1194-1203 (2013).
    • (2013) J. Bacteriol. , vol.195 , Issue.6 , pp. 1194-1203
    • Katayama, Y.1    Baba, T.2    Sekine, M.3    Fukuda, M.4    Hiramatsu, K.5
  • 81
    • 79952263266 scopus 로고    scopus 로고
    • Degradation of fibrinogen and collagen by staphopains, cysteine proteases released from Staphylococcus aureus
    • Ohbayashi T, Irie A, Murakami Y et al. Degradation of fibrinogen and collagen by staphopains, cysteine proteases released from Staphylococcus aureus. Microbiology 157, 786-792 (2011).
    • (2011) Microbiology , vol.157 , pp. 786-792
    • Ohbayashi, T.1    Irie, A.2    Murakami, Y.3
  • 82
    • 3242781863 scopus 로고    scopus 로고
    • Growth phase-dependent production of a cell wall-Associated elastinolytic cysteine proteinase by Staphylococcus epidermidis
    • Oleksy A, Golonka E, Banbula A et al. Growth phase-dependent production of a cell wall-Associated elastinolytic cysteine proteinase by Staphylococcus epidermidis. Biol. Chem. 385(6), 525-535 (2004).
    • (2004) Biol. Chem. , vol.385 , Issue.6 , pp. 525-535
    • Oleksy, A.1    Golonka, E.2    Banbula, A.3
  • 83
    • 0034000130 scopus 로고    scopus 로고
    • Bacterial interference among nasal inhabitants: Eradication of Staphylococcus aureus from nasal cavities by artificial implantation of Corynebacterium sp
    • Uehara Y, Nakama H, Agematsu K et al. Bacterial interference among nasal inhabitants: Eradication of Staphylococcus aureus from nasal cavities by artificial implantation of Corynebacterium sp. J. Hosp. Infect. 44(2), 127-133 (2000).
    • (2000) J. Hosp. Infect. , vol.44 , Issue.2 , pp. 127-133
    • Uehara, Y.1    Nakama, H.2    Agematsu, K.3
  • 84
    • 77952723375 scopus 로고    scopus 로고
    • Staphylococcus epidermidis Esp inhibits Staphylococcus aureus biofilm formation and nasal colonization
    • Iwase T, Uehara Y, Shinji H et al. Staphylococcus epidermidis Esp inhibits Staphylococcus aureus biofilm formation and nasal colonization. Nature 465(7296), 346-349 (2010).
    • (2010) Nature , vol.465 , Issue.7296 , pp. 346-349
    • Iwase, T.1    Uehara, Y.2    Shinji, H.3
  • 85
    • 78651385735 scopus 로고    scopus 로고
    • Staphylococcus aureus hijacks a skin commensal to intensify its virulence: Immunization targeting beta-hemolysin and CAMP factor
    • Lo C, Lai Y, Liu Y, Gallo R, Huang C. Staphylococcus aureus hijacks a skin commensal to intensify its virulence: Immunization targeting beta-hemolysin and CAMP factor. J. Invest. Dermatol. 131(2), 401-409 (2011).
    • (2011) J. Invest. Dermatol. , vol.131 , Issue.2 , pp. 401-409
    • Lo, C.1    Lai, Y.2    Liu, Y.3    Gallo, R.4    Huang, C.5
  • 86
    • 77955708980 scopus 로고    scopus 로고
    • Activation of TLR2 by a small molecule produced by Staphylococcus epidermidis increases antimicrobial defense against bacterial skin infections
    • Lai Y, Cogen A, Radek K et al. Activation of TLR2 by a small molecule produced by Staphylococcus epidermidis increases antimicrobial defense against bacterial skin infections. J. Invest. Dermatol. 130(9), 2211-2221 (2010).
    • (2010) J. Invest. Dermatol. , vol.130 , Issue.9 , pp. 2211-2221
    • Lai, Y.1    Cogen, A.2    Radek, K.3
  • 87
    • 80053603864 scopus 로고    scopus 로고
    • Intranasal application of S epidermidis prevents colonization by methicillin-resistant Staphylococcus aureus in mice
    • Park B, Iwase T, Liu G. Intranasal application of S. epidermidis prevents colonization by methicillin-resistant Staphylococcus aureus in mice. PLoS ONE 6(10), e25880 (2011).
    • (2011) PLoS ONE , vol.6 , Issue.10
    • Park, B.1    Iwase, T.2    Liu, G.3
  • 88
    • 77649121135 scopus 로고    scopus 로고
    • Staphylococcus epidermidis antimicrobial delta-Toxin (phenol-soluble modulin-gamma) cooperates with host antimicrobial peptides to kill group A Streptococcus
    • Cogen A, Yamasaki K, Muto J et al. Staphylococcus epidermidis antimicrobial delta-Toxin (phenol-soluble modulin-gamma) cooperates with host antimicrobial peptides to kill group A Streptococcus. PLoS ONE 5(1), e8557 (2010).
    • (2010) PLoS ONE , vol.5 , Issue.1
    • Cogen, A.1    Yamasaki, K.2    Muto, J.3
  • 89
    • 72049093749 scopus 로고    scopus 로고
    • Selective antimicrobial action is provided by phenol-soluble modulins derived from Staphylococcus epidermidis, a normal resident of the skin
    • Cogen A, Yamasaki K, Sanchez K et al. Selective antimicrobial action is provided by phenol-soluble modulins derived from Staphylococcus epidermidis, a normal resident of the skin. J. Invest. Dermatol. 130(1), 192-200 (2010).
    • (2010) J. Invest. Dermatol. , vol.130 , Issue.1 , pp. 192-200
    • Cogen, A.1    Yamasaki, K.2    Sanchez, K.3
  • 90
    • 84878457632 scopus 로고    scopus 로고
    • Phenol-soluble modulins in staphylococci: What are they originally for?
    • Periasamy S, Chatterjee S, Cheung G, Otto M. Phenol-soluble modulins in staphylococci: What are they originally for?. Commun. Integr. Biol. 5(3), 275-277 (2012).
    • (2012) Commun. Integr. Biol. , vol.5 , Issue.3 , pp. 275-277
    • Periasamy, S.1    Chatterjee, S.2    Cheung, G.3    Otto, M.4
  • 91
    • 84873805850 scopus 로고    scopus 로고
    • Distinct roles of phenol-soluble modulins in spreading of Staphylococcus aureus on wet surfaces
    • Tsompanidou E, Denham E, Becher D et al. Distinct roles of phenol-soluble modulins in spreading of Staphylococcus aureus on wet surfaces. Appl. Environ. Microbiol. 79, 886-895 (2013).
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 886-895
    • Tsompanidou, E.1    Denham, E.2    Becher, D.3
  • 92
    • 0041621569 scopus 로고    scopus 로고
    • PH directly regulates epidermal permeability barrier homeostasis, and stratum corneum integrity/cohesion
    • Hachem J, Crumrine D, Fluhr J, Brown B, Feingold K, Elias P. pH directly regulates epidermal permeability barrier homeostasis, and stratum corneum integrity/cohesion. J. Invest. Dermatol. 121(2), 345-353 (2003).
    • (2003) J. Invest. Dermatol. , vol.121 , Issue.2 , pp. 345-353
    • Hachem, J.1    Crumrine, D.2    Fluhr, J.3    Brown, B.4    Feingold, K.5    Elias, P.6
  • 93
    • 37249053783 scopus 로고    scopus 로고
    • The role of epidermal lipids in cutaneous permeability barrier homeostasis
    • Feingold K. The role of epidermal lipids in cutaneous permeability barrier homeostasis. J. Lipid Res. 48(12), 2531-2546 (2007).
    • (2007) J. Lipid Res. , vol.48 , Issue.12 , pp. 2531-2546
    • Feingold, K.1
  • 94
    • 26444570089 scopus 로고    scopus 로고
    • Sustained serine proteases activity by prolonged increase in pH leads to degradation of lipid processing enzymes and profound alterations of barrier function and stratum corneum integrity
    • Hachem J, Man M, Crumrine D et al. Sustained serine proteases activity by prolonged increase in pH leads to degradation of lipid processing enzymes and profound alterations of barrier function and stratum corneum integrity. J. Invest. Dermatol. 125(3), 510-520 (2005).
    • (2005) J. Invest. Dermatol. , vol.125 , Issue.3 , pp. 510-520
    • Hachem, J.1    Man, M.2    Crumrine, D.3
  • 95
    • 0020615145 scopus 로고
    • Human stratum corneum lipids - characterization and regional variations
    • Lampe M, Burlingame A, Whitney J et al. Human stratum corneum lipids - characterization and regional variations. J. Lipid Res. 24(2), 120-130 (1983).
    • (1983) J. Lipid Res. , vol.24 , Issue.2 , pp. 120-130
    • Lampe, M.1    Burlingame, A.2    Whitney, J.3
  • 96
    • 0014188813 scopus 로고
    • Carriage of staphylococcus aureus in random samples of a normal population
    • Noble W, Valkenburg HA, Wolters C. Carriage of Staphylococcus aureus in random samples of a normal population. J. Hyg. Cambridge 65(4), 567-573 (1967).
    • (1967) J. Hyg. Cambridge , vol.65 , Issue.4 , pp. 567-573
    • Noble, W.1    Valkenburg, H.A.2    Wolters, C.3
  • 97
    • 0016213066 scopus 로고
    • Staphylococcus aureus in lesions of atopic dermatitis
    • Leyden J, Marples R, Kligman A. Staphylococcus aureus in lesions of atopic dermatitis. Br. J. Dermatol. 90(5), 525-530 (1974).
    • (1974) Br. J. Dermatol. , vol.90 , Issue.5 , pp. 525-530
    • Leyden, J.1    Marples, R.2    Kligman, A.3
  • 98
    • 0036062279 scopus 로고    scopus 로고
    • Staphylococcus aureus: Colonizing features and influence of an antibacterial treatment in adults with atopic dermatitis
    • Breuer K, Haussler S, Kapp A, Werfel T. Staphylococcus aureus: Colonizing features and influence of an antibacterial treatment in adults with atopic dermatitis. Br. J. Dermatol. 147(1), 55-61 (2002).
    • (2002) Br. J. Dermatol. , vol.147 , Issue.1 , pp. 55-61
    • Breuer, K.1    Haussler, S.2    Kapp, A.3    Werfel, T.4
  • 99
    • 76849111851 scopus 로고    scopus 로고
    • Antibacterial free fatty acids: Activities, mechanisms of action and biotechnological potential
    • Desbois A, Smith V. Antibacterial free fatty acids: Activities, mechanisms of action and biotechnological potential. Appl. Microbiol. Biotechnol. 85(6), 1629-1642 (2010).
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , Issue.6 , pp. 1629-1642
    • Desbois, A.1    Smith, V.2
  • 100
    • 0015730503 scopus 로고
    • Effect of long-chain fatty acids on bacterial respiration and amino acid uptake
    • Galbrait H, Miller T. Effect of long-chain fatty acids on bacterial respiration and amino acid uptake. J. Appl. Bacteriol. 36(4), 659-675 (1973).
    • (1973) J. Appl. Bacteriol. , vol.36 , Issue.4 , pp. 659-675
    • Galbrait, H.1    Miller, T.2
  • 101
    • 0018642933 scopus 로고
    • Mechanism of the inhibitory action of linoleic acid on the growth of Staphylococcus aureus
    • Greenway D, Dyke K. Mechanism of the inhibitory action of linoleic acid on the growth of Staphylococcus aureus. J. Gen. Microbiol. 115(1), 233-245 (1979).
    • (1979) J. Gen. Microbiol. , vol.115 , Issue.1 , pp. 233-245
    • Greenway, D.1    Dyke, K.2
  • 102
    • 84868308568 scopus 로고    scopus 로고
    • Membrane disruption by antimicrobial fatty acids releases low-molecular-weight proteins from Staphylococcus aureus
    • Parsons J, Yao J, Frank M, Jackson P, Rock C. Membrane disruption by antimicrobial fatty acids releases low-molecular-weight proteins from Staphylococcus aureus. J. Bacteriol. 194(19), 5294-5304 (2012).
    • (2012) J. Bacteriol. , vol.194 , Issue.19 , pp. 5294-5304
    • Parsons, J.1    Yao, J.2    Frank, M.3    Jackson, P.4    Rock, C.5
  • 103
    • 84866723093 scopus 로고    scopus 로고
    • Induction of the staphylococcal proteolytic cascade by antimicrobial fatty acids in community acquired methicillin resistant Staphylococcus aureus
    • Arsic B, Zhu Y, Heinrichs D, McGavin M. Induction of the staphylococcal proteolytic cascade by antimicrobial fatty acids in community acquired methicillin resistant Staphylococcus aureus. PLoS ONE 7(9), e45952 (2012).
    • (2012) PLoS ONE , vol.7 , Issue.9
    • Arsic, B.1    Zhu, Y.2    Heinrichs, D.3    McGavin, M.4
  • 104
    • 67649413346 scopus 로고    scopus 로고
    • Wall teichoic acid protects Staphylococcus aureus against antimicrobial fatty acids from human skin
    • Kohler T, Weidenmaier C, Peschel A. Wall teichoic acid protects Staphylococcus aureus against antimicrobial fatty acids from human skin. J. Bacteriol. 191(13), 4482-4484 (2009).
    • (2009) J. Bacteriol. , vol.191 , Issue.13 , pp. 4482-4484
    • Kohler, T.1    Weidenmaier, C.2    Peschel, A.3
  • 105
    • 34248214172 scopus 로고    scopus 로고
    • The Staphylococcus aureus surface protein IsdA mediates resistance to innate defenses of human skin
    • Clarke S, Mohamed R, Bian L et al. The Staphylococcus aureus surface protein IsdA mediates resistance to innate defenses of human skin. Cell Host Microbe 1(3), 199-212 (2007).
    • (2007) Cell Host Microbe , vol.1 , Issue.3 , pp. 199-212
    • Clarke, S.1    Mohamed, R.2    Bian, L.3
  • 106
    • 84887212397 scopus 로고    scopus 로고
    • The Staphylococcus aureus response to unsaturated long-chain free fatty acids: Survival mechanisms and virulence implications
    • Kenny J, Ward D, Josefsson E et al. The Staphylococcus aureus response to unsaturated long-chain free fatty acids: Survival mechanisms and virulence implications. PLoS ONE 4(2), e4344 (2009).
    • (2009) PLoS ONE , vol.4 , Issue.2
    • Kenny, J.1    Ward, D.2    Josefsson, E.3
  • 107
    • 84855719825 scopus 로고    scopus 로고
    • Characterisation of a cell wall-Anchored protein of Staphylococcus saprophyticus associated with linoleic acid resistance
    • King N, Sakinc T, Ben Zakour N et al. Characterisation of a cell wall-Anchored protein of Staphylococcus saprophyticus associated with linoleic acid resistance. BMC Microbiol. 12, 8 (2012).
    • (2012) BMC Microbiol , vol.12 , pp. 8
    • King, N.1    Sakinc, T.2    Ben Zakour, N.3
  • 108
    • 0025720474 scopus 로고
    • Correlation of carotenoid production, decreased membrane fluidity and resistance to oleic acid killing in Staphylococcus aureus 18Z
    • Chamberlain N, Mehrtens B, Xiong Z, Kapral F, Boardman J, Rearick J. Correlation of carotenoid production, decreased membrane fluidity and resistance to oleic acid killing in Staphylococcus aureus 18Z. Infect. Immun. 59(12), 4332-4337 (1991).
    • (1991) Infect. Immun. , vol.59 , Issue.12 , pp. 4332-4337
    • Chamberlain, N.1    Mehrtens, B.2    Xiong, Z.3    Kapral, F.4    Boardman, J.5    Rearick, J.6
  • 109
    • 33746601080 scopus 로고    scopus 로고
    • Staphyloxanthin plays a role in the fitness of Staphylococcus aureus and its ability to cope with oxidative stress
    • Clauditz A, Resch A, Wieland K, Peschel A, Goetz F. Staphyloxanthin plays a role in the fitness of Staphylococcus aureus and its ability to cope with oxidative stress. Infect. Immun. 74(8), 4950-4953 (2006).
    • (2006) Infect. Immun. , vol.74 , Issue.8 , pp. 4950-4953
    • Clauditz, A.1    Resch, A.2    Wieland, K.3    Peschel, A.4    Goetz, F.5
  • 110
    • 78751693008 scopus 로고    scopus 로고
    • Carotenoid-related alteration of cell membrane fluidity impacts Staphylococcus aureus susceptibility to host defense peptides
    • Mishra N, Liu G, Yeaman M et al. Carotenoid-related alteration of cell membrane fluidity impacts Staphylococcus aureus susceptibility to host defense peptides. Antimicrob. Agents Chemother. 55(2), 526-531 (2011).
    • (2011) Antimicrob. Agents Chemother. , vol.55 , Issue.2 , pp. 526-531
    • Mishra, N.1    Liu, G.2    Yeaman, M.3
  • 111
    • 0030797804 scopus 로고    scopus 로고
    • Characterisation and expression of fatty acid modifying enzyme produced by Staphylococcus epidermidis
    • Chamberlain N, Brueggemann S. Characterisation and expression of fatty acid modifying enzyme produced by Staphylococcus epidermidis. J. Med. Microbiol. 46(8), 693-697 (1997).
    • (1997) J. Med. Microbiol. , vol.46 , Issue.8 , pp. 693-697
    • Chamberlain, N.1    Brueggemann, S.2
  • 112
    • 0026706956 scopus 로고
    • The esterification of fatty acids by Staphylococcus aureus fatty acid modifying enzyme (FAME) and its inhibition by glycerides
    • Kapral F, Smith S, Lal D. The esterification of fatty acids by Staphylococcus aureus fatty acid modifying enzyme (FAME) and its inhibition by glycerides. J. Med. Microbiol. 37(4), 235-237 (1992).
    • (1992) J. Med. Microbiol. , vol.37 , Issue.4 , pp. 235-237
    • Kapral, F.1    Smith, S.2    Lal, D.3
  • 113
    • 0026706955 scopus 로고
    • The production of fatty acid modifying enzyme (FAME) and lipase by various staphylococcal species
    • Long J, Hart J, Albers W, Kapral F. The production of fatty acid modifying enzyme (FAME) and lipase by various staphylococcal species. J. Med. Microbiol. 37(4), 232-234 (1992).
    • (1992) J. Med. Microbiol. , vol.37 , Issue.4 , pp. 232-234
    • Long, J.1    Hart, J.2    Albers, W.3    Kapral, F.4
  • 114
    • 0020626056 scopus 로고
    • In vitro response of Staphylococcus aureus from cystic fibrosis patients to combinations of linoleic and oleic acids added to the nutrient medium
    • Campbell I, Crozier D, Pawagi A, Buivids I. In vitro response of Staphylococcus aureus from cystic fibrosis patients to combinations of linoleic and oleic acids added to the nutrient medium. J. Clin. Microbiol. 18(2), 408-415 (1983).
    • (1983) J. Clin. Microbiol. , vol.18 , Issue.2 , pp. 408-415
    • Campbell, I.1    Crozier, D.2    Pawagi, A.3    Buivids, I.4
  • 115
    • 77951209821 scopus 로고    scopus 로고
    • Myosin cross-reactive antigen of Streptococcus pyogenes M49 encodes a fatty acid double bond hydratase that plays a role in oleic acid detoxification and bacterial virulence
    • Volkov A, Liavonchanka A, Kamneva O et al. Myosin cross-reactive antigen of Streptococcus pyogenes M49 encodes a fatty acid double bond hydratase that plays a role in oleic acid detoxification and bacterial virulence. J. Biol. Chem. 285(14), 10353-10361 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.14 , pp. 10353-10361
    • Volkov, A.1    Liavonchanka, A.2    Kamneva, O.3
  • 116
    • 51449114084 scopus 로고    scopus 로고
    • Thematic review series: Sphingolipids - biodiversity of sphingoid bases ("sphingosines") and related amino alcohols
    • Pruett S, Bushnev A, Hagedorn K et al. Thematic review series: Sphingolipids - biodiversity of sphingoid bases ("sphingosines") and related amino alcohols. J. Lipid Res. 49(8), 1621-1639 (2008).
    • (2008) J. Lipid Res. , vol.49 , Issue.8 , pp. 1621-1639
    • Pruett, S.1    Bushnev, A.2    Hagedorn, K.3
  • 118
    • 0036036354 scopus 로고    scopus 로고
    • Decreased levels of sphingosine, a natural antimicrobial agent, may be associated with vulnerability of the stratum corneum from patients with atopic dermatitis to colonization by Staphylococcus aureus
    • Arikawa J, Ishibashi M, Kawashima M, Takagi Y, Ichikawa Y, Imokawa G. Decreased levels of sphingosine, a natural antimicrobial agent, may be associated with vulnerability of the stratum corneum from patients with atopic dermatitis to colonization by Staphylococcus aureus. J. Invest. Dermatol. 119(2), 433-439 (2002).
    • (2002) J. Invest. Dermatol. , vol.119 , Issue.2 , pp. 433-439
    • Arikawa, J.1    Ishibashi, M.2    Kawashima, M.3    Takagi, Y.4    Ichikawa, Y.5    Imokawa, G.6
  • 119
    • 33644659999 scopus 로고    scopus 로고
    • Complete genome sequence of USA300, an epidemic clone of community-Acquired methicillin-resistant Staphylococcus aureus
    • Diep B, Gill S, Chang R et al. Complete genome sequence of USA300, an epidemic clone of community-Acquired methicillin-resistant Staphylococcus aureus. Lancet 367(9512), 731-739 (2006).
    • (2006) Lancet , vol.367 , Issue.9512 , pp. 731-739
    • Diep, B.1    Gill, S.2    Chang, R.3
  • 120
    • 77955640954 scopus 로고    scopus 로고
    • Arginine catabolic mobile element is associated with low antibiotic resistance and low pathogenicity in Staphylococcus epidermidis from neonates
    • Granslo H, Klingenberg C, Fredheim E, Ronnestad A, Mollnes T, Flaegstad T. Arginine catabolic mobile element is associated with low antibiotic resistance and low pathogenicity in Staphylococcus epidermidis from neonates. Pediatr. Res. 68(3), 237-241 (2010).
    • (2010) Pediatr. Res. , vol.68 , Issue.3 , pp. 237-241
    • Granslo, H.1    Klingenberg, C.2    Fredheim, E.3    Ronnestad, A.4    Mollnes, T.5    Flaegstad, T.6
  • 121
    • 84872512073 scopus 로고    scopus 로고
    • Functional modularity of the arginine catabolic mobile element contributes to the success of USA300 methicillin-resistant Staphylococcus aureus
    • Thurlow L, Joshi G, Clark J et al. Functional modularity of the arginine catabolic mobile element contributes to the success of USA300 methicillin-resistant Staphylococcus aureus. Cell Host Microbe 13(1), 100-107 (2013).
    • (2013) Cell Host Microbe , vol.13 , Issue.1 , pp. 100-107
    • Thurlow, L.1    Joshi, G.2    Clark, J.3
  • 122
    • 67349261301 scopus 로고    scopus 로고
    • Prevalence of the ica operon and insertion sequence IS256 among Staphylococcus epidermidis prosthetic joint infection isolates
    • Koskela A, Nilsdotter-Augustinsson A, Persson L, Soderquist B. Prevalence of the ica operon and insertion sequence IS256 among Staphylococcus epidermidis prosthetic joint infection isolates. Eur. J. Clin. Microbiol. Infect. Dis. 28(6), 655-660 (2009).
    • (2009) Eur. J. Clin. Microbiol. Infect. Dis. , vol.28 , Issue.6 , pp. 655-660
    • Koskela, A.1    Nilsdotter-Augustinsson, A.2    Persson, L.3    Soderquist, B.4
  • 123
    • 63849141377 scopus 로고    scopus 로고
    • Bacterial pleomorphism and competition in a relative humidity gradient
    • de Goffau M, Yang X, van Dijl J, Harmsen H. Bacterial pleomorphism and competition in a relative humidity gradient. Environ. Microbiol. 11(4), 809-822 (2009).
    • (2009) Environ. Microbiol. , vol.11 , Issue.4 , pp. 809-822
    • De Goffau, M.1    Yang, X.2    Van Dijl, J.3    Harmsen, H.4
  • 124
    • 80051952778 scopus 로고    scopus 로고
    • Microbial growth on the edge of desiccation
    • de Goffau M, van Dijl J, Harmsen H. Microbial growth on the edge of desiccation. Environ. Microbiol. 13(8), 2328-2335 (2011).
    • (2011) Environ. Microbiol. , vol.13 , Issue.8 , pp. 2328-2335
    • De Goffau, M.1    Van Dijl, J.2    Harmsen, H.3
  • 125
    • 79251644430 scopus 로고    scopus 로고
    • Desiccation tolerance in Staphylococcus aureus
    • Chaibenjawong P, Foster S. Desiccation tolerance in Staphylococcus aureus. Arch. Microbiol. 193(2), 125-135 (2011).
    • (2011) Arch. Microbiol. , vol.193 , Issue.2 , pp. 125-135
    • Chaibenjawong, P.1    Foster, S.2
  • 126
    • 0026615649 scopus 로고
    • Relationship between desiccation and exopolysaccharide production in a soil pseudomonas species
    • Roberson E, Firestone M. Relationship between desiccation and exopolysaccharide production in a soil pseudomonas species. Appl. Environ. Microbiol. 58(4), 1284-1291 (1992).
    • (1992) Appl. Environ. Microbiol. , vol.58 , Issue.4 , pp. 1284-1291
    • Roberson, E.1    Firestone, M.2
  • 127
    • 48349124615 scopus 로고    scopus 로고
    • Staphylococcus aureus giant protein Ebh is involved in tolerance to transient hyperosmotic pressure
    • Kuroda M, Tanaka Y, Aoki R, Shu D, Tsumoto K, Ohta T. Staphylococcus aureus giant protein Ebh is involved in tolerance to transient hyperosmotic pressure. Biochem. Biophys. Res. Commun. 374(2), 237-241 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.374 , Issue.2 , pp. 237-241
    • Kuroda, M.1    Tanaka, Y.2    Aoki, R.3    Shu, D.4    Tsumoto, K.5    Ohta, T.6
  • 128
    • 78651399469 scopus 로고    scopus 로고
    • Staphylococcus aureus requires cardiolipin for survival under conditions of high salinity
    • Tsai M, Ohniwa R, Kato Y et al. Staphylococcus aureus requires cardiolipin for survival under conditions of high salinity. BMC Microbiol. 11(13), (2011).
    • (2011) BMC Microbiol. , vol.11 , Issue.13
    • Tsai, M.1    Ohniwa, R.2    Kato, Y.3
  • 129
    • 70349526143 scopus 로고    scopus 로고
    • Cardiolipin and the osmotic stress responses of bacteria
    • Romantsov T, Guan Z, Wood J. Cardiolipin and the osmotic stress responses of bacteria. Biochim. Biophys. Acta Biomembranes 1788(10), 2092-2100 (2009).
    • (2009) Biochim. Biophys. Acta Biomembranes , vol.1788 , Issue.10 , pp. 2092-2100
    • Romantsov, T.1    Guan, Z.2    Wood, J.3
  • 130
    • 0032769107 scopus 로고    scopus 로고
    • Functional analysis of the Staphylococcus aureus collagen adhesin B domain
    • Snodgrass J, Mohamed N, Ross J, Sau S, Lee C, Smeltzer M. Functional analysis of the Staphylococcus aureus collagen adhesin B domain. Infect. Immun. 67(8), 3952-3959 (1999).
    • (1999) Infect. Immun. , vol.67 , Issue.8 , pp. 3952-3959
    • Snodgrass, J.1    Mohamed, N.2    Ross, J.3    Sau, S.4    Lee, C.5    Smeltzer, M.6
  • 131
    • 33646561277 scopus 로고    scopus 로고
    • The anchorless adhesin Eap (extracellular adherence protein) from Staphylococcus aureus selectively recognizes extracellular matrix aggregates but binds promiscuously to monomeric matrix macromolecules
    • Hansen U, Hussain M, Villone D et al. The anchorless adhesin Eap (extracellular adherence protein) from Staphylococcus aureus selectively recognizes extracellular matrix aggregates but binds promiscuously to monomeric matrix macromolecules. Matrix Biol. 25(4), 252-260 (2006).
    • (2006) Matrix Biol. , vol.25 , Issue.4 , pp. 252-260
    • Hansen, U.1    Hussain, M.2    Villone, D.3
  • 132
    • 0035164511 scopus 로고    scopus 로고
    • Identification and characterization of a novel 38.5 kilodalton cell surface protein of Staphylococcus aureus with extended spectrum binding activity for extracellular matrix and plasma proteins
    • Hussain M, Becker K, von Eiff C, Schrenzel J, Peters G, Herrmann M. Identification and characterization of a novel 38.5 kilodalton cell surface protein of Staphylococcus aureus with extended spectrum binding activity for extracellular matrix and plasma proteins. J. Bacteriol. 183(23), 6778-6786 (2001).
    • (2001) J. Bacteriol. , vol.183 , Issue.23 , pp. 6778-6786
    • Hussain, M.1    Becker, K.2    Von Eiff, C.3    Schrenzel, J.4    Peters, G.5    Herrmann, M.6
  • 133
    • 0037044740 scopus 로고    scopus 로고
    • Is the GehD lipase from Staphylococcus epidermidis a collagen binding adhesin?
    • Bowden M, Visai L, Longshaw C, Holland KT, Speziale P, Hook M. Is the GehD lipase from Staphylococcus epidermidis a collagen binding adhesin?. J. Biol. Chem. 277(45), 43017-43023 (2002).
    • (2002) J. Biol. Chem. , vol.277 , Issue.45 , pp. 43017-43023
    • Bowden, M.1    Visai, L.2    Longshaw, C.3    Holland, K.T.4    Speziale, P.5    Hook, M.6
  • 134
    • 34547093892 scopus 로고    scopus 로고
    • SdrF, a Staphylococcus epidermidis surface protein, binds type I collagen
    • Arrecubieta C, Lee M, Macey A, Foster T, Lowy F. SdrF, a Staphylococcus epidermidis surface protein, binds type I collagen. J. Biol. Chem. 282(26), 18767-18776 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.26 , pp. 18767-18776
    • Arrecubieta, C.1    Lee, M.2    Macey, A.3    Foster, T.4    Lowy, F.5
  • 135
    • 33746642519 scopus 로고    scopus 로고
    • SdrI, a serine-Aspartate repeat protein identified in Staphylococcus saprophyticus strain 7108, is a collagen-binding protein
    • Sakinc T, Kleine B, Gatermann S. SdrI, a serine-Aspartate repeat protein identified in Staphylococcus saprophyticus strain 7108, is a collagen-binding protein. Infect. Immun. 74(8), 4615-4623 (2006).
    • (2006) Infect. Immun. , vol.74 , Issue.8 , pp. 4615-4623
    • Sakinc, T.1    Kleine, B.2    Gatermann, S.3
  • 136
    • 0036854622 scopus 로고    scopus 로고
    • Staphylococcus aureus clumping factor B (ClfB) promotes adherence to human type I cytokeratin 10: Implications for nasal colonization
    • O'Brien L, Walsh E, Massey R, Peacock S, Foster T. Staphylococcus aureus clumping factor B (ClfB) promotes adherence to human type I cytokeratin 10: Implications for nasal colonization. Cell. Microbiol. 4(11), 759-770 (2002).
    • (2002) Cell. Microbiol. , vol.4 , Issue.11 , pp. 759-770
    • O'Brien, L.1    Walsh, E.2    Massey, R.3    Peacock, S.4    Foster, T.5
  • 137
    • 66549117376 scopus 로고    scopus 로고
    • Iron-regulated surface determinant protein A mediates adhesion of Staphylococcus aureus to human corneocyte envelope proteins
    • Clarke S, Andre G, Walsh E, Dufrene Y, Foster T, Foster S. Iron-regulated surface determinant protein A mediates adhesion of Staphylococcus aureus to human corneocyte envelope proteins. Infect. Immun. 77(6), 2408-2416 (2009).
    • (2009) Infect. Immun. , vol.77 , Issue.6 , pp. 2408-2416
    • Clarke, S.1    Andre, G.2    Walsh, E.3    Dufrene, Y.4    Foster, T.5    Foster, S.6
  • 138
    • 21344433812 scopus 로고    scopus 로고
    • The multifunctional Staphylococcus aureus autolysin Aaa mediates adherence to immobilized fibrinogen and fibronectin
    • Heilmann C, Hartleib J, Hussain M, Peters G. The multifunctional Staphylococcus aureus autolysin Aaa mediates adherence to immobilized fibrinogen and fibronectin. Infect. Immun. 73(8), 4793-4802 (2005).
    • (2005) Infect. Immun. , vol.73 , Issue.8 , pp. 4793-4802
    • Heilmann, C.1    Hartleib, J.2    Hussain, M.3    Peters, G.4
  • 139
    • 78449267357 scopus 로고    scopus 로고
    • A novel staphylococcal internalization mechanism involves the major autolysin Atl and heat shock cognate protein Hsc70 as host cell receptor
    • Hirschhausen N, Schlesier T, Schmidt M, Goetz F, Peters G, Heilmann C. A novel staphylococcal internalization mechanism involves the major autolysin Atl and heat shock cognate protein Hsc70 as host cell receptor. Cell. Microbiol. 12(12), 1746-1764 (2010).
    • (2010) Cell. Microbiol. , vol.12 , Issue.12 , pp. 1746-1764
    • Hirschhausen, N.1    Schlesier, T.2    Schmidt, M.3    Goetz, F.4    Peters, G.5    Heilmann, C.6
  • 140
    • 0028334112 scopus 로고
    • Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus
    • McDevitt D, Francois P, Vaudaux P, Foster T. Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus. Mol. Microbiol. 11(2), 237-248 (1994).
    • (1994) Mol. Microbiol. , vol.11 , Issue.2 , pp. 237-248
    • McDevitt, D.1    Francois, P.2    Vaudaux, P.3    Foster, T.4
  • 141
    • 15444353754 scopus 로고    scopus 로고
    • Clumping factor B (ClfB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus
    • Ni Eidhin D, Perkins S, Francois P, Vaudaux P, Hook M, Foster T. Clumping factor B (ClfB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus. Mol. Microbiol. 30(2), 245-257 (1998).
    • (1998) Mol. Microbiol. , vol.30 , Issue.2 , pp. 245-257
    • Ni Eidhin, D.1    Perkins, S.2    Francois, P.3    Vaudaux, P.4    Hook, M.5    Foster, T.6
  • 142
    • 0034807998 scopus 로고    scopus 로고
    • The Fbe (SdrG) protein of Staphylococcus epidermidis HB promotes bacterial adherence to fibrinogen
    • Hartford O, O'Brien L, Schofield K, Wells J, Foster T. The Fbe (SdrG) protein of Staphylococcus epidermidis HB promotes bacterial adherence to fibrinogen. Microbiology 147, 2545-2552 (2001).
    • (2001) Microbiology , vol.147 , pp. 2545-2552
    • Hartford, O.1    O'Brien, L.2    Schofield, K.3    Wells, J.4    Foster, T.5
  • 144
    • 0034607985 scopus 로고    scopus 로고
    • The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen
    • Wann E, Gurusiddappa S, Hook M. The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen. J. Biol. Chem. 275(18), 13863-13871 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.18 , pp. 13863-13871
    • Wann, E.1    Gurusiddappa, S.2    Hook, M.3
  • 145
    • 79959289525 scopus 로고    scopus 로고
    • The A domain of fibronectin-binding protein B of Staphylococcus aureus contains a novel fibronectin binding site
    • Burke F, Di Poto A, Speziale P, Foster T. The A domain of fibronectin-binding protein B of Staphylococcus aureus contains a novel fibronectin binding site. FEBS J. 278(13), 2359-2371 (2011).
    • (2011) FEBS J. , vol.278 , Issue.13 , pp. 2359-2371
    • Burke, F.1    Di Poto, A.2    Speziale, P.3    Foster, T.4
  • 146
    • 1542407100 scopus 로고    scopus 로고
    • IsdA of Staphylococcus aureus is a broad spectrum, iron-regulated adhesin
    • Clarke S, Wiltshire M, Foster S. IsdA of Staphylococcus aureus is a broad spectrum, iron-regulated adhesin. Mol. Microbiol. 51(5), 1509-1519 (2004).
    • (2004) Mol. Microbiol. , vol.51 , Issue.5 , pp. 1509-1519
    • Clarke, S.1    Wiltshire, M.2    Foster, S.3
  • 147
    • 79953700573 scopus 로고    scopus 로고
    • UafB is a serine-rich repeat adhesin of Staphylococcus saprophyticus that mediates binding to fibronectin, fibrinogen and human uroepithelial cells
    • King N, Beatson S, Totsika M et al. UafB is a serine-rich repeat adhesin of Staphylococcus saprophyticus that mediates binding to fibronectin, fibrinogen and human uroepithelial cells. Microbiology 157, 1161-1175 (2011).
    • (2011) Microbiology , vol.157 , pp. 1161-1175
    • King, N.1    Beatson, S.2    Totsika, M.3
  • 148
    • 0142042875 scopus 로고    scopus 로고
    • Identification and characterization of a novel autolysin (Aae) with adhesive properties from Staphylococcus epidermidis
    • Heilmann C, Thumm G, Chhatwal G, Hartleib J, Uekotter A, Peters G. Identification and characterization of a novel autolysin (Aae) with adhesive properties from Staphylococcus epidermidis. Microbiology 149, 2769-2778 (2003).
    • (2003) Microbiology , vol.149 , pp. 2769-2778
    • Heilmann, C.1    Thumm, G.2    Chhatwal, G.3    Hartleib, J.4    Uekotter, A.5    Peters, G.6
  • 149
    • 0031904826 scopus 로고    scopus 로고
    • Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties
    • Hell W, Meyer H, Gatermann S. Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties. Mol. Microbiol. 29(3), 871-881 (1998).
    • (1998) Mol. Microbiol. , vol.29 , Issue.3 , pp. 871-881
    • Hell, W.1    Meyer, H.2    Gatermann, S.3
  • 150
    • 0037031133 scopus 로고    scopus 로고
    • Several regions of the repeat domain of the Staphylococcus caprae autolysin, At1C, are involved in fibronectin binding
    • Allignet J, England P, Old I, El Solh N. Several regions of the repeat domain of the Staphylococcus caprae autolysin, At1C, are involved in fibronectin binding. FEMS Microbiol. Lett. 213(2), 193-197 (2002).
    • (2002) FEMS Microbiol. Lett. , vol.213 , Issue.2 , pp. 193-197
    • Allignet, J.1    England, P.2    Old, I.3    El Solh, N.4
  • 151
    • 0036892212 scopus 로고    scopus 로고
    • Identification of a fibronectin-binding protein from Staphylococcus epidermidis
    • Williams R, Henderson B, Sharp L, Nair S. Identification of a fibronectin-binding protein from Staphylococcus epidermidis. Infect. Immun. 70(12), 6805-6810 (2002).
    • (2002) Infect. Immun. , vol.70 , Issue.12 , pp. 6805-6810
    • Williams, R.1    Henderson, B.2    Sharp, L.3    Nair, S.4
  • 153
    • 0023391096 scopus 로고
    • Cloning and expression of the gene for a fibronectin-binding protein from Staphylococcus aureus
    • Flock J, Froman G, Jonsson K et al. Cloning and expression of the gene for a fibronectin-binding protein from Staphylococcus aureus. EMBO J. 6(8), 2351-2357 (1987).
    • (1987) EMBO J. , vol.6 , Issue.8 , pp. 2351-2357
    • Flock, J.1    Froman, G.2    Jonsson, K.3
  • 154
    • 0026334144 scopus 로고
    • Two different genes encode fibronectin binding proteins in Staphylococcus aureus -The complete nucleotide sequence and characterization of the 2nd gene
    • Jonsson K, Signas C, Muller H, Lindberg M. Two different genes encode fibronectin binding proteins in Staphylococcus aureus -The complete nucleotide sequence and characterization of the 2nd gene. Eur. J. Biochem. 202(3), 1041-1048 (1991).
    • (1991) Eur. J. Biochem. , vol.202 , Issue.3 , pp. 1041-1048
    • Jonsson, K.1    Signas, C.2    Muller, H.3    Lindberg, M.4
  • 155
    • 71049192313 scopus 로고    scopus 로고
    • SdrI of Staphylococcus saprophyticus is a multifunctional protein: Localization of the fibronectin-binding site
    • Sakinc T, Kleine B, Michalski N, Kaase M, Gatermann S. SdrI of Staphylococcus saprophyticus is a multifunctional protein: Localization of the fibronectin-binding site. FEMS Microbiol. Lett. 301(1), 28-34 (2009).
    • (2009) FEMS Microbiol. Lett. , vol.301 , Issue.1 , pp. 28-34
    • Sakinc, T.1    Kleine, B.2    Michalski, N.3    Kaase, M.4    Gatermann, S.5
  • 156
    • 0036568945 scopus 로고    scopus 로고
    • Adhesion and virulence properties of epidemic Canadian methicillin-resistant Staphylococcus aureus strain 1: Identification of novel adhesion functions associated with plasmin-sensitive surface protein
    • Huesca M, Peralta R, Sauder D, Simor A, McGavin M. Adhesion and virulence properties of epidemic Canadian methicillin-resistant Staphylococcus aureus strain 1: Identification of novel adhesion functions associated with plasmin-sensitive surface protein. J. Infect. Dis. 185(9), 1285-1296 (2002).
    • (2002) J. Infect. Dis. , vol.185 , Issue.9 , pp. 1285-1296
    • Huesca, M.1    Peralta, R.2    Sauder, D.3    Simor, A.4    McGavin, M.5
  • 157
    • 84872035059 scopus 로고    scopus 로고
    • Nasal colonisation by Staphylococcus aureus depends upon clumping factor B binding to the squamous epithelial cell envelope protein loricrin
    • Mulcahy M, Geoghegan J, Monk I et al. Nasal colonisation by Staphylococcus aureus depends upon clumping factor B binding to the squamous epithelial cell envelope protein loricrin. PLoS Pathog. 8(12), e1003092 (2012).
    • (2012) PLoS Pathog , vol.8 , Issue.12
    • Mulcahy, M.1    Geoghegan, J.2    Monk, I.3
  • 158
    • 60749121183 scopus 로고    scopus 로고
    • Surface proteins that promote adherence of Staphylococcus aureus to human desquamated nasal epithelial cells
    • Corrigan R, Miajlovic H, Foster T. Surface proteins that promote adherence of Staphylococcus aureus to human desquamated nasal epithelial cells. BMC Microbiol. 9 (2009).
    • (2009) BMC Microbiol. , vol.9
    • Corrigan, R.1    Miajlovic, H.2    Foster, T.3
  • 159
    • 34547882456 scopus 로고    scopus 로고
    • The role of Staphylococcus aureus surface protein SasG in adherence and biofilm formation
    • Corrigan R, Rigby D, Handley P, Foster T. The role of Staphylococcus aureus surface protein SasG in adherence and biofilm formation. Microbiology 153, 2435-2446 (2007).
    • (2007) Microbiology , vol.153 , pp. 2435-2446
    • Corrigan, R.1    Rigby, D.2    Handley, P.3    Foster, T.4
  • 160
    • 0031663502 scopus 로고    scopus 로고
    • Role of Staphylococcus aureus surface-Associated proteins in the attachment to cultured HaCaT keratinocytes in a new adhesion assay
    • Mempel M, Schmidt T, Weidinger S et al. Role of Staphylococcus aureus surface-Associated proteins in the attachment to cultured HaCaT keratinocytes in a new adhesion assay. J. Invest. Dermatol. 111(3), 452-456 (1998).
    • (1998) J. Invest. Dermatol. , vol.111 , Issue.3 , pp. 452-456
    • Mempel, M.1    Schmidt, T.2    Weidinger, S.3
  • 161
    • 84873105035 scopus 로고    scopus 로고
    • Staphylococcus aureus skin colonization is promoted by barrier disruption and leads to local inflammation
    • Wanke I, Skabytska Y, Kraft B, Peschel A, Biedermann T, Schittek B. Staphylococcus aureus skin colonization is promoted by barrier disruption and leads to local inflammation. Exp. Dermatol. 22(2), 153-155 (2013).
    • (2013) Exp. Dermatol. , vol.22 , Issue.2 , pp. 153-155
    • Wanke, I.1    Skabytska, Y.2    Kraft, B.3    Peschel, A.4    Biedermann, T.5    Schittek, B.6
  • 162
    • 84863877657 scopus 로고    scopus 로고
    • Chronically relapsing pruritic dermatitis in the rats treated as neonate with capsaicin; a potential rat model of human atopic dermatitis
    • Back S, Jeong K, Li C, Lee J, Lee S, Na H. Chronically relapsing pruritic dermatitis in the rats treated as neonate with capsaicin; a potential rat model of human atopic dermatitis. J. Dermatol. Sci. 67(2), 111-119 (2012).
    • (2012) J. Dermatol. Sci. , vol.67 , Issue.2 , pp. 111-119
    • Back, S.1    Jeong, K.2    Li, C.3    Lee, J.4    Lee, S.5    Na, H.6
  • 163
    • 0031952868 scopus 로고    scopus 로고
    • A human-SCID mouse model for allergic immune responses: Bacterial superantigen enhances skin inflammation and suppresses IgE production
    • Herz U, Schnoy N, Borelli S et al. A human-SCID mouse model for allergic immune responses: Bacterial superantigen enhances skin inflammation and suppresses IgE production. J. Invest. Dermatol. 110(3), 224-231 (1998).
    • (1998) J. Invest. Dermatol. , vol.110 , Issue.3 , pp. 224-231
    • Herz, U.1    Schnoy, N.2    Borelli, S.3
  • 164
    • 0032858038 scopus 로고    scopus 로고
    • Development and characterization of a Staphylococcus aureus nasal colonization model in mice
    • Kiser K, Cantey-Kiser J, Lee J. Development and characterization of a Staphylococcus aureus nasal colonization model in mice. Infect. Immun. 67(10), 5001-5006 (1999).
    • (1999) Infect. Immun. , vol.67 , Issue.10 , pp. 5001-5006
    • Kiser, K.1    Cantey-Kiser, J.2    Lee, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.