Abstract
For more than 20 years it is known that β-lactam antibiotics inhibit the transpeptidation of the peptidoglycan [18]. Their primary biochemical targets are some enzymes which are involved in the cross-bridging of the murein peptide sidechains and which are called penicillin binding proteins (PBP’s) [12], for review see Martin et al., [8,13,19].
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Bar-Shavit Z, Goldman R, Ofek I, Sharon N, Mirelman D (1980) Mannose-binding activity of Escherichia coli: a determinant of the attachment and ingestion of bacteria by macrophages. Infect Immun 29: 417–424
Beachey EH, Eisenstein BJ, Ofek I (1980) Sublethal concentrations of antibiotics and bacterial adhesion. In: Elliott K, O’Connor M, Whelan J (eds) Adhesion and microorganism pathogenicity: Ciba foundation symposium 1980. Pitman Medical, London, pp 288–305
Friedman H, Warren GH (1976) Antibody-mediated bacteriolysis: enhanced killing of cyclacillin-treated bacteria. Proc Soc Exp Biol Med 153: 301–304
James R (1975) Identification of an outer membrane protein of Escherichia coli, with a role in the coordination of deoxyribonucleic acid replication and cell elongation. J Bacteriol 124: 918–929
Kroll HP, Bhakdi S, Taylor PW (1983) Membrane changes induced by exposure of Escherichia coli to human serum. Infect Immun 42: 1055–1066
Lugtenberg B, Meijers J, Peters R, Van der Hoek P, Van Alpen L (1975) Electrophoretic resolution of the major outer membrane proteins of Escherichia coli K 12 into four bands FEBS Lett 58: 254–259
Markwell MAK, Haar SM, Bieber LL, Tolbert WE (1978) A modification of the lowry procedure to simplify protein determinations in membrane and lipoprotein samples. Anal Biochem 87: 206–210
Martin HH, Staboulis D, Schilf W (1981) Penicillinbindeproteine der Bakterien als spezifische Wirkorte der β-Laktam-Antibiotika und als Faktoren der Antibiotikaresis¬tenz. Immun Infekt 9: 99–105
Ofek I, Beachey EH, Eisenstein BJ, Alkan MC, Sharon N (1979) Suppression of bacterial adherence by subminimal inhibitory concentrations of ß-lactam and aminoglycoside antibiotics. Rev Inf Dis 1: 832–837
Rogers HJ, Thurman PF (1983) Interrelationships between wall and membrane biosynthesis. In: Hakenbeck R, Höltje JV, Labischinski H (eds) The target of penicillin. Walter de Gruyter, Berlin, New York, pp 637–642
Sandberg T, Stenqvist K, Svanborg-Eden C (1979) Effects of subminimal inhibitory concentrations of ampicillin chloramphenicol and nitrofurantoin on the attachment of Escherichia coli to human uroepithelial cells in vitro. Rev Infect Dis 1: 838–844
Spratt BG (1975) Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Nat Acad Sci USA 72: 2999–3003
Spratt BG (1983) Penicillin-binding proteins and the future of β-lactam antibiotics. J Gen Microbiol 129: 1247–1260
Svanborg-Eden C, Sandberg T, Stenqvist K, Ahlstedt S (1978) Decrease in adhesion of Escherichia coli to human urinary tract epithelial cells in vitro by subinhibitory concentrations of ampicillin. Infection 6, Suppl 1: 121–124
Svanborg-Eden C, Sandberg T, Stenqvist K, Ahlstedt S (1979) Effects of subinhibitory amounts of ampicillin, amoxycillin, and mecillinam on the adhesion of Escherichia coli bacteria to human urinary tract epithelial cells: a preliminary study. Infection 7, Suppl 5: 452–455
Taylor PW, Gaunt H, Unger FM (1981) Effect of subinhibitory concentrations of mecillinam on the serum susceptibility of Escherichia coli strains. Antimicrob Agents Chemother 19: 786–788
Taylor PW, Kroll HP, Tomlinson S (1982) Effect of subinhibitory concentrations of mecillinam on expression of Escherichia coli surface components associated with serum resistance. Drugs Exp Clin Res 8: 625–631
Tipper DJ, Strominger JL (1965) Mechanism of the action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Nat Acad Sci USA 54: 1133–1141
Waxman DJ, Strominger JL (1983) Penicillin-binding proteins and the mechanism of action of ß-lactam antibiotics. Ann Rev Biochem 52: 825–869
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© 1985 Springer-Verlag Berlin Heidelberg
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Leying, H.J., Karch, H., Kroll, H.P., Opferkuch, W. (1985). The Influence of β-Lactam Antibiotics Including Monobactam on the outer and inner Membrane of E. coli . In: Adam, D., Hahn, H., Opferkuch, W. (eds) The Influence of Antibiotics on the Host-Parasite Relationship II. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70748-3_5
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DOI: https://doi.org/10.1007/978-3-642-70748-3_5
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