메뉴 건너뛰기




Volumn 85, Issue 6, 2012, Pages 1119-1132

Cationic antimicrobial peptides disrupt the Streptococcus pyogenes ExPortal

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CATIONIC ANTIMICROBIAL PEPTIDE; CYSTEINE PROTEINASE; CYTOLYSIN; HUMAN NEUTROPHIL PEPTIDE; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN SIC; PROTEIN SPEB; STREPTOLYSIN O; UNCLASSIFIED DRUG;

EID: 84866005675     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08163.x     Document Type: Article
Times cited : (33)

References (61)
  • 2
    • 35548968439 scopus 로고    scopus 로고
    • The role of human innate immune factors in nasal colonization by Staphylococcus aureus
    • van Belkum, A., Emonts, M., Wertheim, H., de Jongh, C., Nouwen, J., Bartels, H., etal. (2007) The role of human innate immune factors in nasal colonization by Staphylococcus aureus. Microbes Infect 9: 1471-1477.
    • (2007) Microbes Infect , vol.9 , pp. 1471-1477
    • van Belkum, A.1    Emonts, M.2    Wertheim, H.3    de Jongh, C.4    Nouwen, J.5    Bartels, H.6
  • 3
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: basic facts and emerging concepts
    • Boman, H.G. (2003) Antibacterial peptides: basic facts and emerging concepts. J Intern Med 254: 197-215.
    • (2003) J Intern Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 4
    • 25444491974 scopus 로고    scopus 로고
    • Keratinocyte production of cathelicidin provides direct activity against bacterial skin pathogens
    • Braff, M.H., Zaiou, M., Fierer, J., Nizet, V., and Gallo, R.L. (2005) Keratinocyte production of cathelicidin provides direct activity against bacterial skin pathogens. Infect Immun 73: 6771-6781.
    • (2005) Infect Immun , vol.73 , pp. 6771-6781
    • Braff, M.H.1    Zaiou, M.2    Fierer, J.3    Nizet, V.4    Gallo, R.L.5
  • 5
    • 0346251029 scopus 로고    scopus 로고
    • Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes
    • Brenot, A., King, K.Y., Janowiak, B., Griffith, O., and Caparon, M.G. (2004) Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes. Infect Immun 72: 408-413.
    • (2004) Infect Immun , vol.72 , pp. 408-413
    • Brenot, A.1    King, K.Y.2    Janowiak, B.3    Griffith, O.4    Caparon, M.G.5
  • 6
    • 12344298832 scopus 로고    scopus 로고
    • The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes
    • Brenot, A., King, K.Y., and Caparon, M.G. (2005) The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes. Mol Microbiol 55: 221-234.
    • (2005) Mol Microbiol , vol.55 , pp. 221-234
    • Brenot, A.1    King, K.Y.2    Caparon, M.G.3
  • 7
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden, K.A. (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3: 238-250.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 10
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham, M.W. (2000) Pathogenesis of group A streptococcal infections. Clin Microbiol Rev 13: 470-511.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 11
    • 9144247030 scopus 로고    scopus 로고
    • The role of lipids in membrane insertion and translocation of bacterial proteins
    • van Dalen, A., and de Kruijff, B. (2004) The role of lipids in membrane insertion and translocation of bacterial proteins. Biochim Biophys Acta 1694: 97-109.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 97-109
    • van Dalen, A.1    de Kruijff, B.2
  • 12
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • Epand, R.M., and Epand, R.F. (2009) Lipid domains in bacterial membranes and the action of antimicrobial agents. Biochim Biophys Acta 1788: 289-294.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 13
    • 79953790729 scopus 로고    scopus 로고
    • Bacterial membrane lipids in the action of antimicrobial agents
    • Epand, R.M., and Epand, R.F. (2011) Bacterial membrane lipids in the action of antimicrobial agents. J Pept Sci 17: 298-305.
    • (2011) J Pept Sci , vol.17 , pp. 298-305
    • Epand, R.M.1    Epand, R.F.2
  • 14
    • 1842684177 scopus 로고    scopus 로고
    • The interaction of streptococcal inhibitor of complement (SIC) and its proteolytic fragments with the human beta defensins
    • Fernie-King, B.A., Seilly, D.J., and Lachmann, P.J. (2004) The interaction of streptococcal inhibitor of complement (SIC) and its proteolytic fragments with the human beta defensins. Immunology 111: 444-452.
    • (2004) Immunology , vol.111 , pp. 444-452
    • Fernie-King, B.A.1    Seilly, D.J.2    Lachmann, P.J.3
  • 16
    • 0037930850 scopus 로고    scopus 로고
    • SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides
    • Frick, I.M., Akesson, P., Rasmussen, M., Schmidtchen, A., and Bjorck, L. (2003) SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides. J Biol Chem 278: 16561-16566.
    • (2003) J Biol Chem , vol.278 , pp. 16561-16566
    • Frick, I.M.1    Akesson, P.2    Rasmussen, M.3    Schmidtchen, A.4    Bjorck, L.5
  • 18
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • Hale, J.D., and Hancock, R.E. (2007) Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev Anti Infect Ther 5: 951-959.
    • (2007) Expert Rev Anti Infect Ther , vol.5 , pp. 951-959
    • Hale, J.D.1    Hancock, R.E.2
  • 19
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock, R.E. (2001) Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect Dis 1: 156-164.
    • (2001) Lancet Infect Dis , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 20
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R.E., and Sahl, H.G. (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24: 1551-1557.
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 21
    • 0026469139 scopus 로고
    • Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells
    • Hanski, E., Horwitz, P.A., and Caparon, M.G. (1992) Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells. Infect Immun 60: 5119-5125.
    • (1992) Infect Immun , vol.60 , pp. 5119-5125
    • Hanski, E.1    Horwitz, P.A.2    Caparon, M.G.3
  • 22
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic
    • Harder, J., Bartels, J., Christophers, E., and Schroder, J.M. (2001) Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic. J Biol Chem 276: 5707-5713.
    • (2001) J Biol Chem , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 23
    • 37349125189 scopus 로고    scopus 로고
    • Sec translocase and sortase A are colocalised in a locus in the cytoplasmic membrane of Streptococcus mutans
    • Hu, P., Bian, Z., Fan, M., Huang, M., and Zhang, P. (2008) Sec translocase and sortase A are colocalised in a locus in the cytoplasmic membrane of Streptococcus mutans. Arch Oral Biol 53: 150-154.
    • (2008) Arch Oral Biol , vol.53 , pp. 150-154
    • Hu, P.1    Bian, Z.2    Fan, M.3    Huang, M.4    Zhang, P.5
  • 25
    • 48849117760 scopus 로고    scopus 로고
    • Cathelicidin LL-37 in severe Streptococcus pyogenes soft tissue infections in humans
    • Johansson, L., Thulin, P., Sendi, P., Hertzen, E., Linder, A., Akesson, P., etal. (2008) Cathelicidin LL-37 in severe Streptococcus pyogenes soft tissue infections in humans. Infect Immun 76: 3399-3404.
    • (2008) Infect Immun , vol.76 , pp. 3399-3404
    • Johansson, L.1    Thulin, P.2    Sendi, P.3    Hertzen, E.4    Linder, A.5    Akesson, P.6
  • 26
    • 77952721475 scopus 로고    scopus 로고
    • Virulence gene regulation by CvfA, a putative RNase: the CvfA-enolase complex in Streptococcus pyogenes links nutritional stress, growth-phase control, and virulence gene expression
    • Kang, S.O., Caparon, M.G., and Cho, K.H. (2010) Virulence gene regulation by CvfA, a putative RNase: the CvfA-enolase complex in Streptococcus pyogenes links nutritional stress, growth-phase control, and virulence gene expression. Infect Immun 78: 2754-2767.
    • (2010) Infect Immun , vol.78 , pp. 2754-2767
    • Kang, S.O.1    Caparon, M.G.2    Cho, K.H.3
  • 27
    • 0142169531 scopus 로고    scopus 로고
    • Lipid binding and membrane penetration of polymyxin B derivatives studied in a biomimetic vesicle system
    • Katz, M., Tsubery, H., Kolusheva, S., Shames, A., Fridkin, M., and Jelinek, R. (2003) Lipid binding and membrane penetration of polymyxin B derivatives studied in a biomimetic vesicle system. Biochem J 375: 405-413.
    • (2003) Biochem J , vol.375 , pp. 405-413
    • Katz, M.1    Tsubery, H.2    Kolusheva, S.3    Shames, A.4    Fridkin, M.5    Jelinek, R.6
  • 28
    • 0242320522 scopus 로고    scopus 로고
    • The bacterial translocase: a dynamic protein channel complex
    • de Keyzer, J., van der Does, C., and Driessen, A.J. (2003) The bacterial translocase: a dynamic protein channel complex. Cell Mol Life Sci 60: 2034-2052.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2034-2052
    • de Keyzer, J.1    van der Does, C.2    Driessen, A.J.3
  • 29
    • 73449109530 scopus 로고    scopus 로고
    • CcpA and LacD.1 affect temporal regulation of Streptococcus pyogenes virulence genes
    • Kietzman, C.C., and Caparon, M.G. (2010) CcpA and LacD.1 affect temporal regulation of Streptococcus pyogenes virulence genes. Infect Immun 78: 241-252.
    • (2010) Infect Immun , vol.78 , pp. 241-252
    • Kietzman, C.C.1    Caparon, M.G.2
  • 30
    • 65549129105 scopus 로고    scopus 로고
    • Mechanism for sortase localization and the role of sortase localization in efficient pilus assembly in Enterococcus faecalis
    • Kline, K.A., Kau, A.L., Chen, S.L., Lim, A., Pinkner, J.S., Rosch, J., etal. (2009) Mechanism for sortase localization and the role of sortase localization in efficient pilus assembly in Enterococcus faecalis. J Bacteriol 191: 3237-3247.
    • (2009) J Bacteriol , vol.191 , pp. 3237-3247
    • Kline, K.A.1    Kau, A.L.2    Chen, S.L.3    Lim, A.4    Pinkner, J.S.5    Rosch, J.6
  • 31
    • 0032030962 scopus 로고    scopus 로고
    • The role of anionic lipids in protein insertion and translocation in bacterial membranes
    • van Klompenburg, W., and de Kruijff, B. (1998) The role of anionic lipids in protein insertion and translocation in bacterial membranes. J Membr Biol 162: 1-7.
    • (1998) J Membr Biol , vol.162 , pp. 1-7
    • van Klompenburg, W.1    de Kruijff, B.2
  • 32
    • 25144519572 scopus 로고    scopus 로고
    • d-alanylation of teichoic acids promotes group A streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion
    • Kristian, S.A., Datta, V., Weidenmaier, C., Kansal, R., Fedtke, I., Peschel, A., etal. (2005) d-alanylation of teichoic acids promotes group A streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion. J Bacteriol 187: 6719-6725.
    • (2005) J Bacteriol , vol.187 , pp. 6719-6725
    • Kristian, S.A.1    Datta, V.2    Weidenmaier, C.3    Kansal, R.4    Fedtke, I.5    Peschel, A.6
  • 33
    • 34248670671 scopus 로고    scopus 로고
    • How group A streptococcus circumvents host phagocyte defenses
    • Kwinn, L.A., and Nizet, V. (2007) How group A streptococcus circumvents host phagocyte defenses. Future Microbiol 2: 75-84.
    • (2007) Future Microbiol , vol.2 , pp. 75-84
    • Kwinn, L.A.1    Nizet, V.2
  • 34
    • 14844351540 scopus 로고    scopus 로고
    • Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection
    • Lee, P.H., Ohtake, T., Zaiou, M., Murakami, M., Rudisill, J.A., Lin, K.H., and Gallo, R.L. (2005) Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection. Proc Natl Acad Sci USA 102: 3750-3755.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3750-3755
    • Lee, P.H.1    Ohtake, T.2    Zaiou, M.3    Murakami, M.4    Rudisill, J.A.5    Lin, K.H.6    Gallo, R.L.7
  • 35
    • 77951271759 scopus 로고    scopus 로고
    • Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II
    • de Leeuw, E., Li, C., Zeng, P., Diepeveen-de Buin, M., Lu, W.Y., Breukink, E., and Lu, W. (2010) Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II. FEBS Lett 584: 1543-1548.
    • (2010) FEBS Lett , vol.584 , pp. 1543-1548
    • de Leeuw, E.1    Li, C.2    Zeng, P.3    Diepeveen-de Buin, M.4    Lu, W.Y.5    Breukink, E.6    Lu, W.7
  • 36
    • 30744463313 scopus 로고    scopus 로고
    • Regulation of SpeB in Streptococcus pyogenes by pH and NaCl: a model for in vivo gene expression
    • Loughman, J.A., and Caparon, M. (2006) Regulation of SpeB in Streptococcus pyogenes by pH and NaCl: a model for in vivo gene expression. J Bacteriol 188: 399-408.
    • (2006) J Bacteriol , vol.188 , pp. 399-408
    • Loughman, J.A.1    Caparon, M.2
  • 37
    • 33751095896 scopus 로고    scopus 로고
    • A novel adaptation of aldolase regulates virulence in Streptococcus pyogenes
    • Loughman, J.A., and Caparon, M.G. (2006) A novel adaptation of aldolase regulates virulence in Streptococcus pyogenes. EMBO J 25: 5414-5422.
    • (2006) EMBO J , vol.25 , pp. 5414-5422
    • Loughman, J.A.1    Caparon, M.G.2
  • 39
    • 1342323730 scopus 로고    scopus 로고
    • Role for serine protease HtrA (DegP) of Streptococcus pyogenes in the biogenesis of virulence factors SpeB and the hemolysin streptolysin S
    • Lyon, W.R., and Caparon, M.G. (2004) Role for serine protease HtrA (DegP) of Streptococcus pyogenes in the biogenesis of virulence factors SpeB and the hemolysin streptolysin S. Infect Immun 72: 1618-1625.
    • (2004) Infect Immun , vol.72 , pp. 1618-1625
    • Lyon, W.R.1    Caparon, M.G.2
  • 40
    • 0032476656 scopus 로고    scopus 로고
    • A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon, W.R., Gibson, C.M., and Caparon, M.G. (1998) A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J 17: 6263-6275.
    • (1998) EMBO J , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 41
    • 65549169236 scopus 로고    scopus 로고
    • vfr, a novel locus affecting cysteine protease production in Streptococcus pyogenes
    • Ma, Y., Bryant, A.E., Salmi, D.B., McIndoo, E., and Stevens, D.L. (2009) vfr, a novel locus affecting cysteine protease production in Streptococcus pyogenes. J Bacteriol 191: 3189-3194.
    • (2009) J Bacteriol , vol.191 , pp. 3189-3194
    • Ma, Y.1    Bryant, A.E.2    Salmi, D.B.3    McIndoo, E.4    Stevens, D.L.5
  • 43
    • 0004294122 scopus 로고    scopus 로고
    • v. (lvi, 1868, 1850] p., 1820] p. of plates). Amsterdam; Boston: Elsevier Academic Press.
    • Mestecky, J. (2005) Mucosal Immunology, p. 2 v. (lvi, 1868, [1850] p., [1820] p. of plates). Amsterdam; Boston: Elsevier Academic Press.
    • (2005) Mucosal Immunology , pp. 2
    • Mestecky, J.1
  • 44
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • Mileykovskaya, E., and Dowhan, W. (2000) Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange. J Bacteriol 182: 1172-1175.
    • (2000) J Bacteriol , vol.182 , pp. 1172-1175
    • Mileykovskaya, E.1    Dowhan, W.2
  • 45
    • 1842456932 scopus 로고    scopus 로고
    • The pathogenesis of streptococcal infections: from tooth decay to meningitis
    • Mitchell, T.J. (2003) The pathogenesis of streptococcal infections: from tooth decay to meningitis. Nat Rev Microbiol 1: 219-230.
    • (2003) Nat Rev Microbiol , vol.1 , pp. 219-230
    • Mitchell, T.J.1
  • 47
    • 0035936156 scopus 로고    scopus 로고
    • Innate antimicrobial peptide protects the skin from invasive bacterial infection
    • Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R.A., etal. (2001) Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 414: 454-457.
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1    Ohtake, T.2    Lauth, X.3    Trowbridge, J.4    Rudisill, J.5    Dorschner, R.A.6
  • 48
    • 38349116218 scopus 로고    scopus 로고
    • Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template'
    • Pag, U., Oedenkoven, M., Sass, V., Shai, Y., Shamova, O., Antcheva, N., etal. (2008) Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template'. J Antimicrob Chemother 61: 341-352.
    • (2008) J Antimicrob Chemother , vol.61 , pp. 341-352
    • Pag, U.1    Oedenkoven, M.2    Sass, V.3    Shai, Y.4    Shamova, O.5    Antcheva, N.6
  • 49
    • 0037330259 scopus 로고    scopus 로고
    • IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes
    • von Pawel-Rammingen, U., and Bjorck, L. (2003) IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes. Curr Opin Microbiol 6: 50-55.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 50-55
    • von Pawel-Rammingen, U.1    Bjorck, L.2
  • 50
    • 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.W., Otto, M., Collins, L.V., Staubitz, P., Nicholson, G., etal. (2001) 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: 1067-1076.
    • (2001) J Exp Med , vol.193 , pp. 1067-1076
    • Peschel, A.1    Jack, R.W.2    Otto, M.3    Collins, L.V.4    Staubitz, P.5    Nicholson, G.6
  • 51
    • 57449114045 scopus 로고    scopus 로고
    • Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane
    • Raz, A., and Fischetti, V.A. (2008) Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane. Proc Natl Acad Sci USA 105: 18549-18554.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18549-18554
    • Raz, A.1    Fischetti, V.A.2
  • 52
    • 2642540881 scopus 로고    scopus 로고
    • A microdomain for protein secretion in Gram-positive bacteria
    • Rosch, J., and Caparon, M. (2004) A microdomain for protein secretion in Gram-positive bacteria. Science 304: 1513-1515.
    • (2004) Science , vol.304 , pp. 1513-1515
    • Rosch, J.1    Caparon, M.2
  • 53
    • 27944484031 scopus 로고    scopus 로고
    • The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes
    • Rosch, J.W., and Caparon, M.G. (2005) The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes. Mol Microbiol 58: 959-968.
    • (2005) Mol Microbiol , vol.58 , pp. 959-968
    • Rosch, J.W.1    Caparon, M.G.2
  • 54
    • 33846603187 scopus 로고    scopus 로고
    • Anionic lipids enriched at the ExPortal of Streptococcus pyogenes
    • Rosch, J.W., Hsu, F.F., and Caparon, M.G. (2007) Anionic lipids enriched at the ExPortal of Streptococcus pyogenes. J Bacteriol 189: 801-806.
    • (2007) J Bacteriol , vol.189 , pp. 801-806
    • Rosch, J.W.1    Hsu, F.F.2    Caparon, M.G.3
  • 55
    • 46249119973 scopus 로고    scopus 로고
    • The signal recognition particle pathway is required for virulence in Streptococcus pyogenes
    • Rosch, J.W., Vega, L.A., Beyer, J.M., Lin, A., and Caparon, M.G. (2008) The signal recognition particle pathway is required for virulence in Streptococcus pyogenes. Infect Immun 76: 2612-2619.
    • (2008) Infect Immun , vol.76 , pp. 2612-2619
    • Rosch, J.W.1    Vega, L.A.2    Beyer, J.M.3    Lin, A.4    Caparon, M.G.5
  • 56
    • 0035923586 scopus 로고    scopus 로고
    • Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway
    • Scott, M.E., Dossani, Z.Y., and Sandkvist, M. (2001) Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway. Proc Natl Acad Sci USA 98: 13978-13983.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13978-13983
    • Scott, M.E.1    Dossani, Z.Y.2    Sandkvist, M.3
  • 57
    • 83355166272 scopus 로고    scopus 로고
    • An amino-terminal signal peptide of Vfr protein negatively influences RopB-dependent SpeB expression and attenuates virulence in Streptococcus pyogenes
    • Shelburne, S.A., 3rd, Olsen, R.J., Makthal, N., Brown, N.G., Sahasrabhojane, P., Watkins, E.M., etal. (2011) An amino-terminal signal peptide of Vfr protein negatively influences RopB-dependent SpeB expression and attenuates virulence in Streptococcus pyogenes. Mol Microbiol 82: 1481-1495.
    • (2011) Mol Microbiol , vol.82 , pp. 1481-1495
    • Shelburne 3rd, S.A.1    Olsen, R.J.2    Makthal, N.3    Brown, N.G.4    Sahasrabhojane, P.5    Watkins, E.M.6
  • 58
    • 33748946749 scopus 로고    scopus 로고
    • Mode of action of the new antibiotic for Gram-positive pathogens daptomycin: comparison with cationic antimicrobial peptides and lipopeptides
    • Straus, S.K., and Hancock, R.E. (2006) Mode of action of the new antibiotic for Gram-positive pathogens daptomycin: comparison with cationic antimicrobial peptides and lipopeptides. Biochim Biophys Acta 1758: 1215-1223.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1215-1223
    • Straus, S.K.1    Hancock, R.E.2
  • 59
    • 33750691343 scopus 로고    scopus 로고
    • The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes
    • Thedieck, K., Hain, T., Mohamed, W., Tindall, B.J., Nimtz, M., Chakraborty, T., etal. (2006) The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes. Mol Microbiol 62: 1325-1339.
    • (2006) Mol Microbiol , vol.62 , pp. 1325-1339
    • Thedieck, K.1    Hain, T.2    Mohamed, W.3    Tindall, B.J.4    Nimtz, M.5    Chakraborty, T.6
  • 60
    • 79960782055 scopus 로고    scopus 로고
    • Antibiotic activities of host defense peptides: more to it than lipid bilayer perturbation
    • Wilmes, M., Cammue, B.P., Sahl, H.G., and Thevissen, K. (2011) Antibiotic activities of host defense peptides: more to it than lipid bilayer perturbation. Nat Prod Rep 28: 1350-1358.
    • (2011) Nat Prod Rep , vol.28 , pp. 1350-1358
    • Wilmes, M.1    Cammue, B.P.2    Sahl, H.G.3    Thevissen, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.