메뉴 건너뛰기




Volumn 103, Issue 5, 1999, Pages 715-721

Cell-wall determinants of the bactericidal action of group IIA phospholipase A2 against Gram-positive bacteria

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; BETA LACTAM ANTIBIOTIC; CEFALOTIN; ERYTHROMYCIN; MEMBRANE PHOSPHOLIPID; PHOSPHOLIPASE A2; VANCOMYCIN;

EID: 0033104949     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI5468     Document Type: Article
Times cited : (88)

References (40)
  • 1
    • 0002282084 scopus 로고
    • Oxygen-independent antimicrobial systems of phagocytes
    • J.I. Gallin, I.M. Goldstein, and R. Snyderman, editors. Raven Press. New York, NY
    • Elsbach, P., and Weiss, J. 1992. Oxygen-independent antimicrobial systems of phagocytes. In inflammation: basic principles and clinical correlates. J.I. Gallin, I.M. Goldstein, and R. Snyderman, editors. Raven Press. New York, NY. 603-636.
    • (1992) Inflammation: Basic Principles and Clinical Correlates , pp. 603-636
    • Elsbach, P.1    Weiss, J.2
  • 2
    • 0001883969 scopus 로고
    • Oxygen metabolites from phagocytes
    • J.I. Gallin, I.M. Goldstein, and R. Snyderman, editors. Raven Press. New York, NY
    • Klebanoff, S.J. 1992. Oxygen metabolites from phagocytes. In Inflammation: basic principles and clinical correlates. J.I. Gallin, I.M. Goldstein, and R. Snyderman, editors. Raven Press. New York, NY. 541-588.
    • (1992) Inflammation: Basic Principles and Clinical Correlates , pp. 541-588
    • Klebanoff, S.J.1
  • 3
    • 0031046654 scopus 로고    scopus 로고
    • Antimicrobial peptides of leukocytes
    • Ganz, T., and Lehrer, R.I. 1997. Antimicrobial peptides of leukocytes. Curr. Opin. Hematol. 4:53-58.
    • (1997) Curr. Opin. Hematol. , vol.4 , pp. 53-58
    • Ganz, T.1    Lehrer, R.I.2
  • 4
    • 0030012702 scopus 로고    scopus 로고
    • Antibiotic proteins of polymorphonuclear leukocytes
    • Levy, O. 1996. Antibiotic proteins of polymorphonuclear leukocytes. Eur. J. Haematol. 56:263-277.
    • (1996) Eur. J. Haematol. , vol.56 , pp. 263-277
    • Levy, O.1
  • 5
    • 0028969853 scopus 로고
    • Extracellular accumulation of potently microbicidal bactericidal/permeability-increasing protein and p15s in an evolving sterile rabbit peritoneal inflammatory exudate
    • Weinrauch, Y., et al. 1995. Extracellular accumulation of potently microbicidal bactericidal/permeability-increasing protein and p15s in an evolving sterile rabbit peritoneal inflammatory exudate. J. Clin. Invest. 95:1916-1924.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1916-1924
    • Weinrauch, Y.1
  • 6
    • 0030070567 scopus 로고    scopus 로고
    • The potent anti-Staphylococcus aureus activity of a sterile rabbit inflammatory fluid is due to a 14-kD phospholipase A2
    • Weinrauch, Y., Elsbach, P., Madsen, L.M., Foreman, A., and Weiss, J. 1996. The potent anti-Staphylococcus aureus activity of a sterile rabbit inflammatory fluid is due to a 14-kD phospholipase A2. J. Clin. Invest. 97:250-257.
    • (1996) J. Clin. Invest. , vol.97 , pp. 250-257
    • Weinrauch, Y.1    Elsbach, P.2    Madsen, L.M.3    Foreman, A.4    Weiss, J.5
  • 7
    • 0001811037 scopus 로고    scopus 로고
    • Biology
    • K.B. Crossley and G.L. Archer, editors. Churchill Livingstone. New York, NY
    • Wilkinson, B.J. 1997. Biology. In The staphylococci in human disease. K.B. Crossley and G.L. Archer, editors. Churchill Livingstone. New York, NY. 1-38.
    • (1997) The Staphylococci in Human Disease , pp. 1-38
    • Wilkinson, B.J.1
  • 8
    • 0014127769 scopus 로고
    • Properties of a cryptic high-frequency transducing phage in Staphylococcus aureus
    • Novick, R. 1967. Properties of a cryptic high-frequency transducing phage in Staphylococcus aureus. Virology. 33:155-166.
    • (1967) Virology , vol.33 , pp. 155-166
    • Novick, R.1
  • 9
    • 0027513024 scopus 로고
    • Isolation and characterization of autolysis-defective mutants of Staphylococcus aureus created by Tn917-lacZ mutagenesis
    • Mani, N., Tobin, P., and Jayaswal, R.K. 1993. Isolation and characterization of autolysis-defective mutants of Staphylococcus aureus created by Tn917-lacZ mutagenesis. J. Bacteriol. 175:1493-1499.
    • (1993) J. Bacteriol. , vol.175 , pp. 1493-1499
    • Mani, N.1    Tobin, P.2    Jayaswal, R.K.3
  • 10
    • 0022894807 scopus 로고
    • Structural and functional properties of a phospholipase A2 purified from an inflammatory exudate
    • Forst, S., et al. 1986. Structural and functional properties of a phospholipase A2 purified from an inflammatory exudate. Biochemistry. 25:8381-8385.
    • (1986) Biochemistry , vol.25 , pp. 8381-8385
    • Forst, S.1
  • 11
    • 0025240360 scopus 로고
    • Purification of a cellular (granulocyte) and an extracellular (serum) phospholipase A2 that participate in the destruction of Escherichia coli in a rabbit inflammatory exudate
    • Wright, G.W., Ooi, C.E., Weiss, J., and Elsbach, P. 1990. Purification of a cellular (granulocyte) and an extracellular (serum) phospholipase A2 that participate in the destruction of Escherichia coli in a rabbit inflammatory exudate. J. Biol. Chem. 265:6675-6681.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6675-6681
    • Wright, G.W.1    Ooi, C.E.2    Weiss, J.3    Elsbach, P.4
  • 12
    • 0025827076 scopus 로고
    • Utilization of labeled Escherichia coli as phospholipase substrate
    • Elsbach, P., and Weiss, J. 1991. Utilization of labeled Escherichia coli as phospholipase substrate. Methods Enzymol. 197:24-31.
    • (1991) Methods Enzymol. , vol.197 , pp. 24-31
    • Elsbach, P.1    Weiss, J.2
  • 13
    • 0028032933 scopus 로고
    • Structural determinants of the action against Escherichia coli of a human inflammatory fluid phospholipase A2 in concert with polymorphonuclear leukocytes
    • Weiss, J., Inada, M., Elsbach, P., and Crowl, R.M. 1994. Structural determinants of the action against Escherichia coli of a human inflammatory fluid phospholipase A2 in concert with polymorphonuclear leukocytes. J. Biol. Chem. 269:26331-26337.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26331-26337
    • Weiss, J.1    Inada, M.2    Elsbach, P.3    Crowl, R.M.4
  • 14
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E.S., and Dyer, W.J. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.S.1    Dyer, W.J.2
  • 15
    • 0029994903 scopus 로고    scopus 로고
    • Determinants of activation by complement of group II phospholipase A2 acting against Escherichia coli
    • Madsen, L.M., Inada, M., and Weiss, J. 1996. Determinants of activation by complement of group II phospholipase A2 acting against Escherichia coli. Infect. Immun. 64:2425-2430.
    • (1996) Infect. Immun. , vol.64 , pp. 2425-2430
    • Madsen, L.M.1    Inada, M.2    Weiss, J.3
  • 16
    • 0017818053 scopus 로고
    • Regulation of bacterial cell walls: Correlation between autolytic activity and cell wall turnover in Staphylococcus aureus
    • Wong, W., Chatterjee, A.N., and Young, F.E. 1978. Regulation of bacterial cell walls: correlation between autolytic activity and cell wall turnover in Staphylococcus aureus. J. Bacteriol. 134:555-561.
    • (1978) J. Bacteriol. , vol.134 , pp. 555-561
    • Wong, W.1    Chatterjee, A.N.2    Young, F.E.3
  • 17
    • 0028986933 scopus 로고
    • Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus
    • Sugai, M., et al. 1995. Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus. J. Bacteriol. 177:1491-1496.
    • (1995) J. Bacteriol. , vol.177 , pp. 1491-1496
    • Sugai, M.1
  • 18
    • 0030940552 scopus 로고    scopus 로고
    • Localized perforation of the cell wall by a major autolysin: Atl gene products and the onset of penicillin-induced lysis of Staphylococcus aureus
    • Sugai, M., et al. 1997. Localized perforation of the cell wall by a major autolysin: atl gene products and the onset of penicillin-induced lysis of Staphylococcus aureus. J. Bacteriol. 179:2958-2962.
    • (1997) J. Bacteriol. , vol.179 , pp. 2958-2962
    • Sugai, M.1
  • 19
    • 0029865232 scopus 로고    scopus 로고
    • An autolysin ring associated with cell separation of Staphylococcus aureus
    • Yamada, S., et al. 1996. An autolysin ring associated with cell separation of Staphylococcus aureus. J. Bacteriol. 178:1565-1571.
    • (1996) J. Bacteriol. , vol.178 , pp. 1565-1571
    • Yamada, S.1
  • 20
    • 0020663559 scopus 로고
    • Changes in the chemical structure of walls of Staphylococcus aureus grown in the presence of chloramphenicol
    • Johannsen, L., Labischinski, H., Reinicke, B. and Giesbrecht, P. 1983. Changes in the chemical structure of walls of Staphylococcus aureus grown in the presence of chloramphenicol. FEMS Microbiol. Lett. 16:313-316.
    • (1983) FEMS Microbiol. Lett. , vol.16 , pp. 313-316
    • Johannsen, L.1    Labischinski, H.2    Reinicke, B.3    Giesbrecht, P.4
  • 21
    • 0015935307 scopus 로고
    • Turnover of bacterial cell wall peptidoglycans
    • Boothby, D., et al. 1973. Turnover of bacterial cell wall peptidoglycans. J. Biol. Chem. 248:2161-2169.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2161-2169
    • Boothby, D.1
  • 22
    • 0030044640 scopus 로고    scopus 로고
    • Staphylocidal action of thrombin-induced platelet microbicidal protein is not solely dependent on transmembrane potential
    • Koo, S.P., Bayer, A.S., Sahl, H.G., Proctor, R.A., and Yeaman, M.R. 1996. Staphylocidal action of thrombin-induced platelet microbicidal protein is not solely dependent on transmembrane potential. Infect. Immun. 64:1070-1074.
    • (1996) Infect. Immun. , vol.64 , pp. 1070-1074
    • Koo, S.P.1    Bayer, A.S.2    Sahl, H.G.3    Proctor, R.A.4    Yeaman, M.R.5
  • 23
    • 0015137521 scopus 로고
    • Metabolism of phosphatidylglycerol, lysylphosphatidylglycerol, and cardiolipin of Staphylococcus aureus
    • Short, S.A., and White, D.C. 1971. Metabolism of phosphatidylglycerol, lysylphosphatidylglycerol, and cardiolipin of Staphylococcus aureus. J. Bacteriol. 108:219-226.
    • (1971) J. Bacteriol. , vol.108 , pp. 219-226
    • Short, S.A.1    White, D.C.2
  • 24
    • 0031921754 scopus 로고    scopus 로고
    • Characterization of the starvation-survival response of Staphylococcus aureus
    • Watson, S.P., Clements, M.O., and Foster, S.J. 1998. Characterization of the starvation-survival response of Staphylococcus aureus. J. Bacteriol. 180:1750-1758.
    • (1998) J. Bacteriol. , vol.180 , pp. 1750-1758
    • Watson, S.P.1    Clements, M.O.2    Foster, S.J.3
  • 25
    • 0022652442 scopus 로고
    • The rate of killing of Escherichia coli by beta-lactam antibiotics is strictly proportional to the rate of bacterial growth
    • Tuomanen, E., Cozens, R., Tosch, W., Zak, O., and Tomasz, A. 1986. The rate of killing of Escherichia coli by beta-lactam antibiotics is strictly proportional to the rate of bacterial growth. J. Gen. Microbiol. 132:1297-1304.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 1297-1304
    • Tuomanen, E.1    Cozens, R.2    Tosch, W.3    Zak, O.4    Tomasz, A.5
  • 26
    • 0029739334 scopus 로고    scopus 로고
    • Staphylocidal action of thrombin-induced platelet microbicidal protein is influenced by microenvironment and target cell growth phase
    • Koo, S.P., Yeaman, M.R., and Bayer, A.S. 1996. Staphylocidal action of thrombin-induced platelet microbicidal protein is influenced by microenvironment and target cell growth phase. Infect. Immun. 64:3758-3764.
    • (1996) Infect. Immun. , vol.64 , pp. 3758-3764
    • Koo, S.P.1    Yeaman, M.R.2    Bayer, A.S.3
  • 27
    • 0025894781 scopus 로고
    • Cross-linking and O-acetylation of peptidoglycan in Staphylococcus aureus (strains H and MR-1) grown in the presence of sub-growth-inhibitory concentrations of beta-lactam antibiotics
    • Snowden, M.A., and Perkins, H.R. 1991. Cross-linking and O-acetylation of peptidoglycan in Staphylococcus aureus (strains H and MR-1) grown in the presence of sub-growth-inhibitory concentrations of beta-lactam antibiotics. J. Gen. Microbiol. 137:1661-1666.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 1661-1666
    • Snowden, M.A.1    Perkins, H.R.2
  • 28
    • 0022609126 scopus 로고
    • Effects of growth of methicillin-resistant and -susceptible Staphylococcus aureus in the presence of beta-lactams on peptidoglycan structure and susceptibility to lytic enzymes
    • Qoronfleh, M.W., and Wilkinson, B.J. 1986. Effects of growth of methicillin-resistant and -susceptible Staphylococcus aureus in the presence of beta-lactams on peptidoglycan structure and susceptibility to lytic enzymes. Antimicrob. Agents Chemother. 29:250-257.
    • (1986) Antimicrob. Agents Chemother. , vol.29 , pp. 250-257
    • Qoronfleh, M.W.1    Wilkinson, B.J.2
  • 29
    • 0030049824 scopus 로고    scopus 로고
    • Identification and molecular characterization of a putative regulatory locus that affects autolysis in Staphylococcus aureus
    • Brunskill, E.W., and Bayles, K.W. 1996. Identification and molecular characterization of a putative regulatory locus that affects autolysis in Staphylococcus aureus. J. Bacteriol. 178:611-618.
    • (1996) J. Bacteriol. , vol.178 , pp. 611-618
    • Brunskill, E.W.1    Bayles, K.W.2
  • 30
    • 0028244076 scopus 로고
    • Lipoteichoic acid and lipids in the membrane of Staphylococcus aureus
    • Fischer, W. 1994. Lipoteichoic acid and lipids in the membrane of Staphylococcus aureus. Med. Microbiol. Immunol. 183:61-76.
    • (1994) Med. Microbiol. Immunol. , vol.183 , pp. 61-76
    • Fischer, W.1
  • 31
    • 0017142415 scopus 로고
    • Effect of lipoteichoic acid and lipids on lysis of intact cells of Streptococcus faecalis
    • Cleveland, R.F., Daneo-Moore, L., Wicken, J.A., and Shockman, G.D. 1976. Effect of lipoteichoic acid and lipids on lysis of intact cells of Streptococcus faecalis. J. Bacteriol. 127:1582-1584.
    • (1976) J. Bacteriol. , vol.127 , pp. 1582-1584
    • Cleveland, R.F.1    Daneo-Moore, L.2    Wicken, J.A.3    Shockman, G.D.4
  • 32
    • 0017281745 scopus 로고
    • Inhibition of wall autolysis in Streptococcus faecalis by lipoteichoic acid and lipids
    • Cleveland, R.F., Wicken, A.J., Daneo-Moore, L., and Shockman, G.D. 1976. Inhibition of wall autolysis in Streptococcus faecalis by lipoteichoic acid and lipids. J. Bacteriol. 126:192-197.
    • (1976) J. Bacteriol. , vol.126 , pp. 192-197
    • Cleveland, R.F.1    Wicken, A.J.2    Daneo-Moore, L.3    Shockman, G.D.4
  • 33
    • 0026512822 scopus 로고
    • Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis
    • Foster, S.J. 1992. Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis. J. Bacteriol. 174:464-470.
    • (1992) J. Bacteriol. , vol.174 , pp. 464-470
    • Foster, S.J.1
  • 34
    • 0003838347 scopus 로고
    • Microbial cell walls and membranes
    • Chapman and Hall. London, United Kingdom
    • Rogers H.J., Perkins, H.R., and Ward, J.B. 1980. Microbial cell walls and membranes. In The bacterial autolysins. Chapman and Hall. London, United Kingdom. 437-459.
    • (1980) The Bacterial Autolysins , pp. 437-459
    • Rogers, H.J.1    Perkins, H.R.2    Ward, J.B.3
  • 35
    • 0023514772 scopus 로고
    • The functions of autolysins in the growth and division of Bacillus subtilis
    • Doyle, R.J., and Koch, A.L. 1987. The functions of autolysins in the growth and division of Bacillus subtilis. Crit. Rev. Microbiol. 15:169-222.
    • (1987) Crit. Rev. Microbiol. , vol.15 , pp. 169-222
    • Doyle, R.J.1    Koch, A.L.2
  • 36
    • 0014733740 scopus 로고
    • Model for cell wall growth of Streptococcus faecalis
    • Higgins, M.L., and Shockman, G.D. 1970. Model for cell wall growth of Streptococcus faecalis. J. Bacteriol. 101:643-648.
    • (1970) J. Bacteriol. , vol.101 , pp. 643-648
    • Higgins, M.L.1    Shockman, G.D.2
  • 37
    • 0028872519 scopus 로고
    • Bactericidal properties of murine intestinal phospholipase A2
    • Harwig, S., et al. 1995. Bactericidal properties of murine intestinal phospholipase A2. J. Clin. Invest. 95:603-610.
    • (1995) J. Clin. Invest. , vol.95 , pp. 603-610
    • Harwig, S.1
  • 38
    • 10544223740 scopus 로고    scopus 로고
    • Secretion of type II phospholipase A2 and cryptdin by rat small intestinal Paneth cells
    • Qu, X.D., Lloyd, K.C., Walsh, J.H., and Lehrer, R.I. 1996. Secretion of type II phospholipase A2 and cryptdin by rat small intestinal Paneth cells. Infect. Immun. 64:5161-5165.
    • (1996) Infect. Immun. , vol.64 , pp. 5161-5165
    • Qu, X.D.1    Lloyd, K.C.2    Walsh, J.H.3    Lehrer, R.I.4
  • 39
    • 0031596818 scopus 로고    scopus 로고
    • Secretory phosphohpase A2 is the principal bactericide for staphylococci and other gram-positive bacteria in human tears
    • Qu, X.D., and Lehrer, R.I. 1998. Secretory phosphohpase A2 is the principal bactericide for staphylococci and other gram-positive bacteria in human tears. Infect. Immun. 66:2791-2797.
    • (1998) Infect. Immun. , vol.66 , pp. 2791-2797
    • Qu, X.D.1    Lehrer, R.I.2
  • 40
    • 0032145843 scopus 로고    scopus 로고
    • Mobilization of potent plasma bactericidal activity during systemic bacterial challenge: Role of group IIA phospholipiase A2
    • Weinrauch, Y., Abad, C., Liang, N.-S., Lowry, S.F., and Weiss, J. 1998. Mobilization of potent plasma bactericidal activity during systemic bacterial challenge: role of group IIA phospholipiase A2. J. Clin. Invest. 102:633-638.
    • (1998) J. Clin. Invest. , vol.102 , pp. 633-638
    • Weinrauch, Y.1    Abad, C.2    Liang, N.-S.3    Lowry, S.F.4    Weiss, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.