메뉴 건너뛰기




Volumn 7, Issue 5, 2004, Pages 477-487

Staphylococci in colonization and disease: Prospective targets for drugs and vaccines

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; ANTIBIOTIC AGENT; BINDING PROTEIN; CADAVERINE; CHIMERIC PROTEIN; DNA VACCINE; FIBRONECTIN BINDING PROTEIN; GALLIDERMIN; IMMUNOGLOBULIN; LANTIBIOTIC; LINEZOLID; MANNOPEPTIMYCIN DERIVATIVE; MEMBRANE LIPID; MERSACIDIN; METHIONINE TRANSFER RNA; METICILLIN; MUTANT PROTEIN; NISIN; PEPTIDE DEFORMYLASE; PEPTIDOGLYCAN; PERTUSSIS VACCINE; PLASMID DNA; POLYSACCHARIDE; RAMOPLANIN; SORTASE; STAPHYLOCOCCUS TOXIN; TEICHOIC ACID; TOXIC SHOCK SYNDROME TOXIN 1; UNCLASSIFIED DRUG; UNINDEXED DRUG; VANCOMYCIN;

EID: 4644255644     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2004.08.014     Document Type: Review
Times cited : (56)

References (75)
  • 1
    • 50649102939 scopus 로고    scopus 로고
    • The Genera Staphylococcus and Macrococcus
    • Edited by Dworkin M: Springer; http://141.150.157.117:8080/prokWIP/ chaphtm/8356/COMPLETE.htm. vol Release 3.17.]
    • Götz F, Bannerman T, Schleifer KH: The Genera Staphylococcus and Macrococcus. In The Procaryotes, edn http://141.150.157.117:8080/prokWIP/ chaphtm/356/COMPLETE.htm. Edited by Dworkin M: Springer; 2004: http://141.150.157.117:8080/prokWIP/chaphtm/8356/COMPLETE.htm. vol Release 3.17.]
    • (2004) The Procaryotes, Edn.
    • Götz, F.1    Bannerman, T.2    Schleifer, K.H.3
  • 3
    • 0036792157 scopus 로고    scopus 로고
    • Antimicrobials: New solutions badly needed
    • S.J. Projan, and P.J. Youngman Antimicrobials: new solutions badly needed Curr Opin Microbiol 5 2002 463 465
    • (2002) Curr Opin Microbiol , vol.5 , pp. 463-465
    • Projan, S.J.1    Youngman, P.J.2
  • 5
    • 0942287204 scopus 로고    scopus 로고
    • High level oxacillin and vancomycin resistance and altered cell wall composition in Staphylococcus aureus carrying the staphylococcal mecA and the enterococcal vanA gene complex
    • A. Severin, K. Tabei, F. Tenover, M. Chung, N. Clarke, and A. Tomasz High level oxacillin and vancomycin resistance and altered cell wall composition in Staphylococcus aureus carrying the staphylococcal mecA and the enterococcal vanA gene complex J Biol Chem 279 2004 3398 3407
    • (2004) J Biol Chem , vol.279 , pp. 3398-3407
    • Severin, A.1    Tabei, K.2    Tenover, F.3    Chung, M.4    Clarke, N.5    Tomasz, A.6
  • 6
    • 0037416970 scopus 로고    scopus 로고
    • FemABX peptidyl transferases: A link between branched-chain cell wall peptide formation and beta-lactam resistance in Gram-positive cocci
    • S. Rohrer, and B. Berger-Bächi FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and beta-lactam resistance in Gram-positive cocci Antimicrob Agents Chemother 47 2003 837 846 This article summarizes the results on the pentaglycine bridge formation in S. aureus. The genetic and biochemical evidence suggest that the sequential addition of these glycines is catalyzed by three homologous enzymes, FemX (FmhB), FemA and FemB. These enzymes represent very promising targets for antibiotic design.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 837-846
    • Rohrer, S.1    Berger-Bächi, B.2
  • 8
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • A. Peschel How do bacteria resist human antimicrobial peptides? Trends Microbiol 10 2002 179 186 This review gives an overview on mechanisms that S. aureus and other pathogens are using to resist cationic antimicrobial peptides an important human defense regime.
    • (2002) Trends Microbiol , vol.10 , pp. 179-186
    • Peschel, A.1
  • 9
    • 2342639647 scopus 로고    scopus 로고
    • Role of teichoic acids in Staphylococcus aureus nasal colonization, a major risk factor in nosocomial infections
    • C. Weidenmaier, J.F. Kokai-Kun, S.A. Kristian, T. Chanturiya, H. Kalbacher, M. Gross, G. Nicholson, B. Neumeister, J.J. Mond, and A. Peschel Role of teichoic acids in Staphylococcus aureus nasal colonization, a major risk factor in nosocomial infections Nat Med 10 2004 243 245 This article provides for the first time clear evidences that the wall teichoic acid of S. aureus is a major colonization factor of the anterior nares in a cotton rat nare colonization model.
    • (2004) Nat Med , vol.10 , pp. 243-245
    • Weidenmaier, C.1    Kokai-Kun, J.F.2    Kristian, S.A.3    Chanturiya, T.4    Kalbacher, H.5    Gross, M.6    Nicholson, G.7    Neumeister, B.8    Mond, J.J.9    Peschel, A.10
  • 10
    • 0037099263 scopus 로고    scopus 로고
    • Staphylococcus aureus strains lacking d-alanine modifications of teichoic acids are highly susceptible to human neutrophil killing and are virulence attenuated in mice
    • L.V. Collins, S.A. Kristian, C. Weidenmaier, M. Faigle, K.P. Van Kessel, J.A. Van Strijp, F. Götz, B. Neumeister, and A. Peschel Staphylococcus aureus strains lacking d-alanine modifications of teichoic acids are highly susceptible to human neutrophil killing and are virulence attenuated in mice J Infect Dis 186 2002 214 219 The lack of d-alanine incorporation into teichoic acids in the staphylococcal cell envelope decreases defensin resistance and virulence. Thus the dlt operon represents an interesting target.
    • (2002) J Infect Dis , vol.186 , pp. 214-219
    • Collins, L.V.1    Kristian, S.A.2    Weidenmaier, C.3    Faigle, M.4    Van Kessel, K.P.5    Van Strijp, J.A.6    Götz, F.7    Neumeister, B.8    Peschel, A.9
  • 11
    • 0043159258 scopus 로고    scopus 로고
    • Alanylation of teichoic acids protects Staphylococcus aureus against Toll-like receptor 2-dependent host defense in a mouse tissue cage infection model
    • S.A. Kristian, X. Lauth, V. Nizet, F. Götz, B. Neumeister, A. Peschel, and R. Landmann Alanylation of teichoic acids protects Staphylococcus aureus against Toll-like receptor 2-dependent host defense in a mouse tissue cage infection model J Infect Dis 188 2003 414 423
    • (2003) J Infect Dis , vol.188 , pp. 414-423
    • Kristian, S.A.1    Lauth, X.2    Nizet, V.3    Götz, F.4    Neumeister, B.5    Peschel, A.6    Landmann, R.7
  • 12
    • 84862433005 scopus 로고    scopus 로고
    • Biosynthesis of the lantibiotics epidermin and gallidermin
    • V. Braun F. Götz WILEY-VCH Verlag GmbH
    • F. Götz, and G. Jung Biosynthesis of the lantibiotics epidermin and gallidermin V. Braun F. Götz Microbial fundamentals of biotechnology 2001 WILEY-VCH Verlag GmbH 52 92
    • (2001) Microbial Fundamentals of Biotechnology , pp. 52-92
    • Götz, F.1    Jung, G.2
  • 13
    • 0141988644 scopus 로고    scopus 로고
    • Bacterial resistance to antimicrobial host defenses - An emerging target for novel antiinfective strategies?
    • C. Weidenmaier, S.A. Kristian, and A. Peschel Bacterial resistance to antimicrobial host defenses - an emerging target for novel antiinfective strategies? Curr Drug Targets 4 2003 643 649
    • (2003) Curr Drug Targets , vol.4 , pp. 643-649
    • Weidenmaier, C.1    Kristian, S.A.2    Peschel, A.3
  • 14
    • 0842325226 scopus 로고    scopus 로고
    • MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance
    • P. Staubitz, H. Neumann, T. Schneider, I. Wiedemann, and A. Peschel MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance FEMS Microbiol Lett 231 2004 67 71
    • (2004) FEMS Microbiol Lett , vol.231 , pp. 67-71
    • Staubitz, P.1    Neumann, H.2    Schneider, T.3    Wiedemann, I.4    Peschel, A.5
  • 15
    • 0037218495 scopus 로고    scopus 로고
    • MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing
    • S.A. Kristian, M. Dürr, J.A. Van Strijp, B. Neumeister, and A. Peschel MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing Infect Immun 71 2003 546 549
    • (2003) Infect Immun , vol.71 , pp. 546-549
    • Kristian, S.A.1    Dürr, M.2    Van Strijp, J.A.3    Neumeister, B.4    Peschel, A.5
  • 16
    • 0036271350 scopus 로고    scopus 로고
    • Staphylococcus and biofilms
    • F. Götz Staphylococcus and biofilms Mol Microbiol 43 2002 1367 1378
    • (2002) Mol Microbiol , vol.43 , pp. 1367-1378
    • Götz, F.1
  • 17
    • 0037456641 scopus 로고    scopus 로고
    • Lack of biofilm contribution to bacterial colonisation in an experimental model of foreign body infection by Staphylococcus aureus and Staphylococcus epidermidis
    • P. Francois, P.H. Tu Quoc, C. Bisognano, W.L. Kelley, D.P. Lew, J. Schrenzel, S.E. Cramton, F. Götz, and P. Vaudaux Lack of biofilm contribution to bacterial colonisation in an experimental model of foreign body infection by Staphylococcus aureus and Staphylococcus epidermidis FEMS Immunol Med Microbiol 35 2003 135 140
    • (2003) FEMS Immunol Med Microbiol , vol.35 , pp. 135-140
    • Francois, P.1    Tu Quoc, P.H.2    Bisognano, C.3    Kelley, W.L.4    Lew, D.P.5    Schrenzel, J.6    Cramton, S.E.7    Götz, F.8    Vaudaux, P.9
  • 18
    • 1642303755 scopus 로고    scopus 로고
    • The ability of biofilm formation does not influence virulence of Staphylococcus aureus and host response in a mouse tissue cage infection model
    • S.A. Kristian, T. Golda, F. Ferracin, S.E. Cramton, B. Neumeister, A. Peschel, F. Götz, and R. Landmann The ability of biofilm formation does not influence virulence of Staphylococcus aureus and host response in a mouse tissue cage infection model Microb Pathog 36 2004 237 245
    • (2004) Microb Pathog , vol.36 , pp. 237-245
    • Kristian, S.A.1    Golda, T.2    Ferracin, F.3    Cramton, S.E.4    Neumeister, B.5    Peschel, A.6    Götz, F.7    Landmann, R.8
  • 19
    • 12244255730 scopus 로고    scopus 로고
    • Isolation, structural characterization, and immunological evaluation of a high-molecular-weight exopolysaccharide from Staphylococcus aureus
    • J.G. Joyce, C. Abeygunawardana, Q. Xu, J.C. Cook, R. Hepler, C.T. Przysiecki, K.M. Grimm, K. Roper, C.C. Ip, and L. Cope Isolation, structural characterization, and immunological evaluation of a high-molecular-weight exopolysaccharide from Staphylococcus aureus Carbohydr Res 338 2003 903 922
    • (2003) Carbohydr Res , vol.338 , pp. 903-922
    • Joyce, J.G.1    Abeygunawardana, C.2    Xu, Q.3    Cook, J.C.4    Hepler, R.5    Przysiecki, C.T.6    Grimm, K.M.7    Roper, K.8    Ip, C.C.9    Cope, L.10
  • 20
    • 0036084386 scopus 로고    scopus 로고
    • Increased virulence of a fibronectin-binding protein mutant of Staphylococcus aureus in a rat model of pneumonia
    • M.C. McElroy, D.J. Cain, C. Tyrrell, T.J. Foster, and C. Haslett Increased virulence of a fibronectin-binding protein mutant of Staphylococcus aureus in a rat model of pneumonia Infect Immun 70 2002 3865 3873
    • (2002) Infect Immun , vol.70 , pp. 3865-3873
    • McElroy, M.C.1    Cain, D.J.2    Tyrrell, C.3    Foster, T.J.4    Haslett, C.5
  • 22
    • 0036156141 scopus 로고    scopus 로고
    • Fibronectin-binding proteins of Staphylococcus aureus are involved in adherence to human airway epithelium
    • E. Mongodin, O. Bajolet, J. Cutrona, N. Bonnet, F. Dupuit, E. Puchelle, and S. de Bentzmann Fibronectin-binding proteins of Staphylococcus aureus are involved in adherence to human airway epithelium Infect Immun 70 2002 620 630
    • (2002) Infect Immun , vol.70 , pp. 620-630
    • Mongodin, E.1    Bajolet, O.2    Cutrona, J.3    Bonnet, N.4    Dupuit, F.5    Puchelle, E.6    De Bentzmann, S.7
  • 24
    • 0142042875 scopus 로고    scopus 로고
    • Identification and characterization of a novel autolysin (Aae) with adhesive properties from Staphylococcus epidermidis
    • C. Heilmann, G. Thumm, G.S. Chhatwal, J. Hartleib, A. Uekotter, and G. Peters Identification and characterization of a novel autolysin (Aae) with adhesive properties from Staphylococcus epidermidis Microbiology 149 2003 2769 2778
    • (2003) Microbiology , vol.149 , pp. 2769-2778
    • Heilmann, C.1    Thumm, G.2    Chhatwal, G.S.3    Hartleib, J.4    Uekotter, A.5    Peters, G.6
  • 25
    • 0036893408 scopus 로고    scopus 로고
    • Analysis of Ebh, a 1.1-megadalton cell wall-associated fibronectin-binding protein of Staphylococcus aureus
    • S.R. Clarke, L.G. Harris, R.G. Richards, and S.J. Foster Analysis of Ebh, a 1.1-megadalton cell wall-associated fibronectin-binding protein of Staphylococcus aureus Infect Immun 70 2002 6680 6687
    • (2002) Infect Immun , vol.70 , pp. 6680-6687
    • Clarke, S.R.1    Harris, L.G.2    Richards, R.G.3    Foster, S.J.4
  • 26
    • 2542512497 scopus 로고    scopus 로고
    • Recombinant Streptococcus equi proteins protect mice in challenge experiments and induce immune response in horses
    • M. Flock, K. Jacobsson, L. Frykberg, T.R. Hirst, A. Franklin, B. Guss, and J.I. Flock Recombinant Streptococcus equi proteins protect mice in challenge experiments and induce immune response in horses Infect Immun 72 2004 3228 3236
    • (2004) Infect Immun , vol.72 , pp. 3228-3236
    • Flock, M.1    Jacobsson, K.2    Frykberg, L.3    Hirst, T.R.4    Franklin, A.5    Guss, B.6    Flock, J.I.7
  • 27
    • 1842687784 scopus 로고    scopus 로고
    • Extracellular fibrinogen binding protein, Efb, from Staphylococcus aureus binds to platelets and inhibits platelet aggregation
    • O. Shannon, and J.I. Flock Extracellular fibrinogen binding protein, Efb, from Staphylococcus aureus binds to platelets and inhibits platelet aggregation Thromb Haemost 91 2004 779 789
    • (2004) Thromb Haemost , vol.91 , pp. 779-789
    • Shannon, O.1    Flock, J.I.2
  • 29
    • 12244313428 scopus 로고    scopus 로고
    • A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: Crystal structure of the fibrinogen-binding MSCRAMM, clumping factor a
    • C.C. Deivanayagam, E.R. Wann, W. Chen, M. Carson, K.R. Rajashankar, M. Hook, and S.V. Narayana A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A EMBO J 21 2002 6660 6672 For anti-adhesive drug design it is important to know that the fibrinogen and collagen-binding protein of S. aureus contain similarly folded domains as the immunoglobulin.
    • (2002) EMBO J , vol.21 , pp. 6660-6672
    • Deivanayagam, C.C.1    Wann, E.R.2    Chen, W.3    Carson, M.4    Rajashankar, K.R.5    Hook, M.6    Narayana, S.V.7
  • 30
    • 0142011077 scopus 로고    scopus 로고
    • The Staphylococcus aureus surface protein SasG and its homologues promote bacterial adherence to human desquamated nasal epithelial cells
    • F.M. Roche, M. Meehan, and T.J. Foster The Staphylococcus aureus surface protein SasG and its homologues promote bacterial adherence to human desquamated nasal epithelial cells Microbiology 149 2003 2759 2767
    • (2003) Microbiology , vol.149 , pp. 2759-2767
    • Roche, F.M.1    Meehan, M.2    Foster, T.J.3
  • 31
    • 0242684412 scopus 로고    scopus 로고
    • Extracellular adherence protein from Staphylococcus aureus enhances internalization into eukaryotic cells
    • A. Haggar, M. Hussain, H. Lonnies, M. Herrmann, A. Norrby-Teglund, and J.I. Flock Extracellular adherence protein from Staphylococcus aureus enhances internalization into eukaryotic cells Infect Immun 71 2003 2310 2317
    • (2003) Infect Immun , vol.71 , pp. 2310-2317
    • Haggar, A.1    Hussain, M.2    Lonnies, H.3    Herrmann, M.4    Norrby-Teglund, A.5    Flock, J.I.6
  • 32
    • 0036263195 scopus 로고    scopus 로고
    • Insertional inactivation of Eap in Staphylococcus aureus strain Newman confers reduced staphylococcal binding to fibroblasts
    • M. Hussain, A. Haggar, C. Heilmann, G. Peters, J.I. Flock, and M. Herrmann Insertional inactivation of Eap in Staphylococcus aureus strain Newman confers reduced staphylococcal binding to fibroblasts Infect Immun 70 2000 2933 2940
    • (2000) Infect Immun , vol.70 , pp. 2933-2940
    • Hussain, M.1    Haggar, A.2    Heilmann, C.3    Peters, G.4    Flock, J.I.5    Herrmann, M.6
  • 36
    • 3543073805 scopus 로고    scopus 로고
    • Crystal structures of Staphylococcus aureus sortase a and its substrate complex
    • Y. Zong, T.W. Bice, H. Ton-That, O. Schneewind, and S.V. Narayana Crystal structures of Staphylococcus aureus sortase A and its substrate complex J Biol Chem 279 2004 31383 31389
    • (2004) J Biol Chem , vol.279 , pp. 31383-31389
    • Zong, Y.1    Bice, T.W.2    Ton-That, H.3    Schneewind, O.4    Narayana, S.V.5
  • 38
    • 1642534360 scopus 로고    scopus 로고
    • The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall
    • Y. Zong, S.K. Mazmanian, O. Schneewind, and S.V. Narayana The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall Structure (Camb) 12 2004 105 112
    • (2004) Structure (Camb) , vol.12 , pp. 105-112
    • Zong, Y.1    Mazmanian, S.K.2    Schneewind, O.3    Narayana, S.V.4
  • 39
    • 0037093930 scopus 로고    scopus 로고
    • On the role of Staphylococcus aureus sortase and sortase-catalyzed surface protein anchoring in murine septic arthritis
    • I.M. Jonsson, S.K. Mazmanian, O. Schneewind, M. Verdrengh, T. Bremell, and A. Tarkowski On the role of Staphylococcus aureus sortase and sortase-catalyzed surface protein anchoring in murine septic arthritis J Infect Dis 185 2002 1417 1424
    • (2002) J Infect Dis , vol.185 , pp. 1417-1424
    • Jonsson, I.M.1    Mazmanian, S.K.2    Schneewind, O.3    Verdrengh, M.4    Bremell, T.5    Tarkowski, A.6
  • 40
    • 0141614012 scopus 로고    scopus 로고
    • Staphylococcus aureus alpha-toxin induces apoptosis in peripheral blood mononuclear cells: Role of endogenous tumour necrosis factor-alpha and the mitochondrial death pathway
    • B. Haslinger, K. Strangfeld, G. Peters, K. Schulze-Osthoff, and B. Sinha Staphylococcus aureus alpha-toxin induces apoptosis in peripheral blood mononuclear cells: role of endogenous tumour necrosis factor-alpha and the mitochondrial death pathway Cell Microbiol 5 2003 729 741
    • (2003) Cell Microbiol , vol.5 , pp. 729-741
    • Haslinger, B.1    Strangfeld, K.2    Peters, G.3    Schulze-Osthoff, K.4    Sinha, B.5
  • 41
    • 0141809842 scopus 로고    scopus 로고
    • Staphylococcus aureus alpha-toxin-induced cell death: Predominant necrosis despite apoptotic caspase activation
    • F. Essmann, H. Bantel, G. Totzke, I.H. Engels, B. Sinha, K. Schulze-Osthoff, and R.U. Janicke Staphylococcus aureus alpha-toxin-induced cell death: predominant necrosis despite apoptotic caspase activation Cell Death Differ 10 2003 1260 1272
    • (2003) Cell Death Differ , vol.10 , pp. 1260-1272
    • Essmann, F.1    Bantel, H.2    Totzke, G.3    Engels, I.H.4    Sinha, B.5    Schulze-Osthoff, K.6    Janicke, R.U.7
  • 43
    • 2442650172 scopus 로고    scopus 로고
    • High resolution crystallographic studies of {alpha}-hemolysin- phospholipid complexes define heptamer-lipid head group interactions: Implication for understanding protein-lipid interactions
    • S. Galdiero, and E. Gouaux High resolution crystallographic studies of {alpha}-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: Implication for understanding protein-lipid interactions Protein Sci 13 2004 1503 1511
    • (2004) Protein Sci , vol.13 , pp. 1503-1511
    • Galdiero, S.1    Gouaux, E.2
  • 44
    • 0345791535 scopus 로고    scopus 로고
    • Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus alpha-toxin and beta-toxin
    • P.W. Park, T.J. Foster, E. Nishi, S.J. Duncan, M. Klagsbrun, and Y. Chen Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus alpha-toxin and beta-toxin J Biol Chem 279 2004 251 258
    • (2004) J Biol Chem , vol.279 , pp. 251-258
    • Park, P.W.1    Foster, T.J.2    Nishi, E.3    Duncan, S.J.4    Klagsbrun, M.5    Chen, Y.6
  • 45
    • 0242593842 scopus 로고    scopus 로고
    • Life-threatening hemoptysis in adults with community-acquired pneumonia due to Panton-Valentine leukocidin-secreting Staphylococcus aureus
    • V. Boussaud, A. Parrot, C. Mayaud, M. Wislez, M. Antoine, C. Picard, F. Delisle, J. Etienne, and J. Cadranel Life-threatening hemoptysis in adults with community-acquired pneumonia due to Panton-Valentine leukocidin-secreting Staphylococcus aureus Intensive Care Med 29 2003 1840 1843
    • (2003) Intensive Care Med , vol.29 , pp. 1840-1843
    • Boussaud, V.1    Parrot, A.2    Mayaud, C.3    Wislez, M.4    Antoine, M.5    Picard, C.6    Delisle, F.7    Etienne, J.8    Cadranel, J.9
  • 46
    • 0037006653 scopus 로고    scopus 로고
    • Association between Staphylococcus aureus strains carrying gene for Panton-Valentine leukocidin and highly lethal necrotising pneumonia in young immunocompetent patients
    • Y. Gillet, B. Issartel, P. Vanhems, J.C. Fournet, G. Lina, M. Bes, F. Vandenesch, Y. Piemont, N. Brousse, and D. Floret Association between Staphylococcus aureus strains carrying gene for Panton-Valentine leukocidin and highly lethal necrotising pneumonia in young immunocompetent patients Lancet 359 2002 753 759
    • (2002) Lancet , vol.359 , pp. 753-759
    • Gillet, Y.1    Issartel, B.2    Vanhems, P.3    Fournet, J.C.4    Lina, G.5    Bes, M.6    Vandenesch, F.7    Piemont, Y.8    Brousse, N.9    Floret, D.10
  • 47
    • 0037242676 scopus 로고    scopus 로고
    • Purification, cloning and characterization of variant LukE-LukD with strong leukocidal activity of staphylococcal bi-component leukotoxin family
    • N. Morinaga, Y. Kaihou, and M. Noda Purification, cloning and characterization of variant LukE-LukD with strong leukocidal activity of staphylococcal bi-component leukotoxin family Microbiol Immunol 47 2003 81 90
    • (2003) Microbiol Immunol , vol.47 , pp. 81-90
    • Morinaga, N.1    Kaihou, Y.2    Noda, M.3
  • 49
    • 0042346160 scopus 로고    scopus 로고
    • Functional analysis of the TCR binding domain of toxic shock syndrome toxin-1 predicts further diversity in MHC class II/superantigen/TCR ternary complexes
    • J.K. McCormick, T.J. Tripp, A.S. Llera, E.J. Sundberg, M.M. Dinges, R.A. Mariuzza, and P.M. Schlievert Functional analysis of the TCR binding domain of toxic shock syndrome toxin-1 predicts further diversity in MHC class II/superantigen/TCR ternary complexes J Immunol 171 2003 1385 1392
    • (2003) J Immunol , vol.171 , pp. 1385-1392
    • McCormick, J.K.1    Tripp, T.J.2    Llera, A.S.3    Sundberg, E.J.4    Dinges, M.M.5    Mariuzza, R.A.6    Schlievert, P.M.7
  • 50
    • 0141835875 scopus 로고    scopus 로고
    • Vaccination with nontoxic mutant toxic shock syndrome toxin 1 protects against Staphylococcus aureus infection
    • D.L. Hu, K. Omoe, S. Sasaki, H. Sashinami, H. Sakuraba, Y. Yokomizo, K. Shinagawa, and A. Nakane Vaccination with nontoxic mutant toxic shock syndrome toxin 1 protects against Staphylococcus aureus infection J Infect Dis 188 2003 743 752
    • (2003) J Infect Dis , vol.188 , pp. 743-752
    • Hu, D.L.1    Omoe, K.2    Sasaki, S.3    Sashinami, H.4    Sakuraba, H.5    Yokomizo, Y.6    Shinagawa, K.7    Nakane, A.8
  • 51
    • 1242326951 scopus 로고    scopus 로고
    • Staphylococcus aureus and food poisoning
    • Y. Le Loir, F. Baron, and M. Gautier Staphylococcus aureus and food poisoning Genet Mol Res 2 2003 63 76
    • (2003) Genet Mol Res , vol.2 , pp. 63-76
    • Le Loir, Y.1    Baron, F.2    Gautier, M.3
  • 52
    • 2442684023 scopus 로고    scopus 로고
    • Enterotoxin B is the predominant toxin involved in staphylococcal scarlet Fever in Taiwan
    • C.C. Wang, W.T. Lo, C.F. Hsu, and M.L. Chu Enterotoxin B is the predominant toxin involved in staphylococcal scarlet Fever in Taiwan Clin Infect Dis 38 2004 1498 1502
    • (2004) Clin Infect Dis , vol.38 , pp. 1498-1502
    • Wang, C.C.1    Lo, W.T.2    Hsu, C.F.3    Chu, M.L.4
  • 53
    • 1542298940 scopus 로고    scopus 로고
    • Antibodies to highly conserved peptide sequence of staphylococcal and streptococcal superantigens in Kawasaki disease
    • M. Gupta-Malhotra, A. Viteri-Jackson, W. Thomas, and J.B. Zabriskie Antibodies to highly conserved peptide sequence of staphylococcal and streptococcal superantigens in Kawasaki disease Exp Mol Pathol 76 2004 117 121
    • (2004) Exp Mol Pathol , vol.76 , pp. 117-121
    • Gupta-Malhotra, M.1    Viteri-Jackson, A.2    Thomas, W.3    Zabriskie, J.B.4
  • 54
    • 1242272034 scopus 로고    scopus 로고
    • Design of chimeric receptor mimics with different TcRVbeta isoforms. Type-specific inhibition of superantigen pathogenesis
    • E. Hong-Geller, M. Mollhoff, P.R. Shiflett, and G. Gupta Design of chimeric receptor mimics with different TcRVbeta isoforms. Type-specific inhibition of superantigen pathogenesis J Biol Chem 279 2004 5676 5684
    • (2004) J Biol Chem , vol.279 , pp. 5676-5684
    • Hong-Geller, E.1    Mollhoff, M.2    Shiflett, P.R.3    Gupta, G.4
  • 55
    • 0036307873 scopus 로고    scopus 로고
    • Molecular mechanisms of blister formation in bullous impetigo and staphylococcal scalded skin syndrome
    • Y. Hanakawa, N.M. Schechter, C. Lin, L. Garza, H. Li, T. Yamaguchi, Y. Fudaba, K. Nishifuji, M. Sugai, and M. Amagai Molecular mechanisms of blister formation in bullous impetigo and staphylococcal scalded skin syndrome J Clin Invest 110 2002 53 60 Exfoliative toxins of S. aureus are responsible for the staphylococcal scalded skin syndrome, a blistering skin disorder. The verification as the glutamate-specific trypsin-like serine protease and the identification of its target desmoglein-51, a desmosomal glycoprotein, is a major brake through in finding new antitoxin strategies for the treatment and prevention of the staphylococcal scalded skin syndrome.
    • (2002) J Clin Invest , vol.110 , pp. 53-60
    • Hanakawa, Y.1    Schechter, N.M.2    Lin, C.3    Garza, L.4    Li, H.5    Yamaguchi, T.6    Fudaba, Y.7    Nishifuji, K.8    Sugai, M.9    Amagai, M.10
  • 57
    • 1542347211 scopus 로고    scopus 로고
    • Cloning and sequence analysis of genes encoding Staphylococcus hyicus exfoliative toxin types A, B, C, and D
    • P. Ahrens, and L.O. Andresen Cloning and sequence analysis of genes encoding Staphylococcus hyicus exfoliative toxin types A, B, C, and D J Bacteriol 186 2004 1833 1837
    • (2004) J Bacteriol , vol.186 , pp. 1833-1837
    • Ahrens, P.1    Andresen, L.O.2
  • 58
    • 0242475185 scopus 로고    scopus 로고
    • Understanding the mechanism of action of the exfoliative toxins of Staphylococcus aureus
    • S. Ladhani Understanding the mechanism of action of the exfoliative toxins of Staphylococcus aureus FEMS Immunol Med Microbiol 39 2003 181 189
    • (2003) FEMS Immunol Med Microbiol , vol.39 , pp. 181-189
    • Ladhani, S.1
  • 59
    • 0036848132 scopus 로고    scopus 로고
    • Nisin, alone and combined with peptidoglycan-modulating antibiotics: Activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci
    • W. Brumfitt, M.R. Salton, and J.M. Hamilton-Miller Nisin, alone and combined with peptidoglycan-modulating antibiotics: activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci J Antimicrob Chemother 50 2002 731 734
    • (2002) J Antimicrob Chemother , vol.50 , pp. 731-734
    • Brumfitt, W.1    Salton, M.R.2    Hamilton-Miller, J.M.3
  • 60
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • I. Wiedemann, E. Breukink, C. van Kraaij, O.P. Kuipers, G. Bierbaum, B. de Kruijff, and H.G. Sahl Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity J Biol Chem 276 2001 1772 1779
    • (2001) J Biol Chem , vol.276 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    Van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    De Kruijff, B.6    Sahl, H.G.7
  • 64
    • 1442324697 scopus 로고    scopus 로고
    • Interactions between penicillin-binding proteins (PBPs) and two novel classes of PBP inhibitors, arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones
    • A. Zervosen, W.P. Lu, Z. Chen, R.E. White, T.P. Demuth Jr., and J.M. Frere Interactions between penicillin-binding proteins (PBPs) and two novel classes of PBP inhibitors, arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones Antimicrob Agents Chemother 48 2004 961 969
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 961-969
    • Zervosen, A.1    Lu, W.P.2    Chen, Z.3    White, R.E.4    Demuth Jr., T.P.5    Frere, J.M.6
  • 65
    • 0038364156 scopus 로고    scopus 로고
    • Cathelicidins-a family of multifunctional antimicrobial peptides
    • R. Bals, and J.M. Wilson Cathelicidins-a family of multifunctional antimicrobial peptides Cell Mol Life Sci 60 2003 711 720
    • (2003) Cell Mol Life Sci , vol.60 , pp. 711-720
    • Bals, R.1    Wilson, J.M.2
  • 66
    • 0038041942 scopus 로고    scopus 로고
    • Minidefensins and other antimicrobial peptides: Candidate anti-HIV microbicides
    • A.M. Cole Minidefensins and other antimicrobial peptides: candidate anti-HIV microbicides Expert Opin Ther Targets 7 2003 329 341
    • (2003) Expert Opin Ther Targets , vol.7 , pp. 329-341
    • Cole, A.M.1
  • 67
    • 1642475071 scopus 로고    scopus 로고
    • Staphylococcus aureus capsular polysaccharides
    • K. O'Riordan, and J.C. Lee Staphylococcus aureus capsular polysaccharides Clin Microbiol Rev 17 2004 218 234 This review gives a excellent insight into the biosynthesis and role in virulence of the predominant serotype 215 and 218 capsular polysaccharides of S. aureus. These polysaccharides are the basis of an effective S. aureus vaccine.
    • (2004) Clin Microbiol Rev , vol.17 , pp. 218-234
    • O'Riordan, K.1    Lee, J.C.2
  • 68
    • 0036084114 scopus 로고    scopus 로고
    • Overproduction of type 8 capsular polysaccharide augments Staphylococcus aureus virulence
    • T.T. Luong, and C.Y. Lee Overproduction of type 8 capsular polysaccharide augments Staphylococcus aureus virulence Infect Immun 70 2002 3389 3395
    • (2002) Infect Immun , vol.70 , pp. 3389-3395
    • Luong, T.T.1    Lee, C.Y.2
  • 69
    • 0842346288 scopus 로고    scopus 로고
    • Development of StaphVAX, a polysaccharide conjugate vaccine against S. aureus infection: From the lab bench to phase III clinical trials
    • A.I. Fattom, G. Horwith, S. Fuller, M. Propst, and R. Naso Development of StaphVAX, a polysaccharide conjugate vaccine against S. aureus infection: from the lab bench to phase III clinical trials Vaccine 22 2004 880 887 The vaccine is based on the two most prevalent capsular polysaccharides, types 885 and 888, of S. aureus. It is interesting that this conjugate vaccine promotes a Th882 response.
    • (2004) Vaccine , vol.22 , pp. 880-887
    • Fattom, A.I.1    Horwith, G.2    Fuller, S.3    Propst, M.4    Naso, R.5
  • 70
    • 10744232525 scopus 로고    scopus 로고
    • Characterization of a protective monoclonal antibody recognizing Staphylococcus aureus MSCRAMM protein clumping factor a
    • A.E. Hall, P.J. Domanski, P.R. Patel, J.H. Vernachio, P.J. Syribeys, E.L. Gorovits, M.A. Johnson, J.M. Ross, J.T. Hutchins, and J.M. Patti Characterization of a protective monoclonal antibody recognizing Staphylococcus aureus MSCRAMM protein clumping factor A Infect Immun 71 2003 6864 6870 It has long been known that the fibrinogen binding protein ClfA plays a role in S. aureus virulence and cell invasion. The protective role of monoclonal antibody in a murine sepsis model corroborates the importance of this virulence factor.
    • (2003) Infect Immun , vol.71 , pp. 6864-6870
    • Hall, A.E.1    Domanski, P.J.2    Patel, P.R.3    Vernachio, J.H.4    Syribeys, P.J.5    Gorovits, E.L.6    Johnson, M.A.7    Ross, J.M.8    Hutchins, J.T.9    Patti, J.M.10
  • 71
    • 1442323885 scopus 로고    scopus 로고
    • Expression of staphylococcal clumping factor a impedes macrophage phagocytosis
    • N. Palmqvist, J.M. Patti, A. Tarkowski, and E. Josefsson Expression of staphylococcal clumping factor A impedes macrophage phagocytosis Microbes Infect 6 2004 188 195
    • (2004) Microbes Infect , vol.6 , pp. 188-195
    • Palmqvist, N.1    Patti, J.M.2    Tarkowski, A.3    Josefsson, E.4
  • 72
    • 0035925904 scopus 로고    scopus 로고
    • Whole genome sequencing of methicillin-resistant Staphylococcus aureus
    • M. Kuroda, T. Ohta, I. Uchiyama, T. Baba, H. Yuzawa, I. Kobayashi, L. Cui, A. Oguchi, K. Aoki, and Y. Nagai Whole genome sequencing of methicillin-resistant Staphylococcus aureus Lancet 357 2001 1225 1240 This is the publication of the first Staphylococcus genomes. This paper marks a milestone in staphylococcal genome and virulence analysis.
    • (2001) Lancet , vol.357 , pp. 1225-1240
    • Kuroda, M.1    Ohta, T.2    Uchiyama, I.3    Baba, T.4    Yuzawa, H.5    Kobayashi, I.6    Cui, L.7    Oguchi, A.8    Aoki, K.9    Nagai, Y.10
  • 73
  • 74
    • 0037417075 scopus 로고    scopus 로고
    • Proteomic approach to understanding antibiotic action
    • J.E. Bandow, H. Brötz, L.I. Leichert, H. Labischinski, and M. Hecker Proteomic approach to understanding antibiotic action Antimicrob Agents Chemother 47 2003 948 955 With proteomic technology it is possible to elucidate the complex cellular responses in bacteria and to obtain information as to the site of action of an unknown antibiotic.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 948-955
    • Bandow, J.E.1    Brötz, H.2    Leichert, L.I.3    Labischinski, H.4    Hecker, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.