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Gene Review

ECs0673  -  penicillin-binding protein 2

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs0673

  • Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole [1].
  • Alterations affecting similar regions of Escherichia coli PBP3 and Neisseria gonorrhoeae PBP2 from beta-lactam-resistant strains are known [2].
  • A novel penicillin-binding protein, PBP-2' (Mr about 75,000), is known to be induced in excessively large amount by most beta-lactam compounds in cells of a clinically isolated strain of Staphylococcus aureus, TK784, that is highly resistant to beta-lactams and also most other antibiotics [3].
  • Penicillin-binding proteins from Erwinia amylovora: mutants lacking PBP2 are avirulent [4].
  • The effect of furazlocillin on the morphology, autolysis, and murein synthesis of E. coli mutants deficient in either PBP-1A, PBP-1Bs, or PBP-2 was studied [5].

High impact information on ECs0673

  • The cross-linking reaction was strongly inhibited by the amidinopenicillin, mecillinam, and by other beta-lactam antibiotics that have a high affinity for PBP-2, but not by beta-lactams that had very low affinity for PBP-2 [6].
  • The formation of peptidoglycan required the presence of high levels of both PBP-2 and the RodA protein in the membranes, but it is unclear which of the two proteins was primarily responsible for the extension of the glycan chains (transglycosylation) [6].
  • The cross-linked peptidoglycan was synthesized from UDP-N-acetylmuramylpentapeptide and UDP-N-acetylglucosamine in the presence of a high concentration of cefmetazole that inhibited all of PBPs except PBP-2 [6].
  • PBP2 localized in the bacterial envelope in a spot-like pattern and also at mid-cell during cell division [1].
  • In contrast to subunits of the divisome, PBP2 failed to localize at mid-cell when PBP3 was inhibited by the specific antibiotic aztreonam [1].

Chemical compound and disease context of ECs0673


Biological context of ECs0673

  • Similar relationships between PBP saturation and killing kinetics were obtained with imipenem and meropenem at concentrations which inhibited only one PBP (PBP 2), only two PBPs (PBP 1s and 2), or all three essential PBPs [11].
  • In this strain, meropenem caused a more than 50% reduction in cell number increase at a concentration very close to the 50% inhibitory concentration for penicillin-binding protein type 2 (PBP 2), whereas imipenem, at the same concentration, did not significantly inhibit cell growth [12].
  • Exposure of the cells to cefotaxime at concentrations at which it bound selectively to PBP 2 resulted in the extrusion of cytoplasm and cell lysis, whereas exposure to cephalexin at concentrations at which it bound exclusively to PBP 3 resulted in cell enlargement and the cessation of septation [13].
  • This DNA was cloned on plasmid pACYC184 and was shown to cause both production of PBP-2' and resistance to tobramycin in Escherichia coli cells [3].
  • The DNA sequence located between mecA, the gene that codes for penicillin-binding protein PBP2', and insertion sequence-like element IS431mec has been termed hypervariable because of its length polymorphism among different staphylococcal isolates [14].

Anatomical context of ECs0673

  • The hydropathy profile suggested that the NH2-terminal hydrophobic region (a stretch of 25 non-ionic amino acids) may anchor PBP 2 in the cytoplasmic membrane as an ectoprotein [15].

Associations of ECs0673 with chemical compounds

  • Cefotaxime binds selectively to PBP 2, and cephalexin binds to PBP 3, each at its respective MIC [13].
  • Saturation of a single PBP by cefsulodin (PBP 1s), mecillinam (PBP 2), and aztreonam (PBP 3) resulted in a slow rate of killing (2.5-, 1.5-, and 0.8-log-unit decreases in the number of CFU per milliliter, respectively, in 6 h) [11].
  • 6059-S had the highest affinity for PBP-3 and -7/8, had a higher affinity than benzylpenicillin for PBP-1A, -1Bs, -4, and -5/6 and a lower affinity for PBP-2, 609134, the 1-thiacephem analog of 6059-S, showed as high an affinity for PBP-1A, -1Bs, -3, and -4 as 6059-S but a lower affinity for PBP-5/6 [16].
  • When the reaction conditions for the radiolabeled penicillin used in this procedure were modified by lowering the temperature (2 degrees C) and reducing the incubation time (3 min), temocillin showed a much higher affinity for PBP-3 and improved affinity for the other PBPs, with the exception of PBP-2 [17].
  • Based on these observations, we concluded that pbpA is essential for the growth of methicillin-sensitive S. aureus [18].

Analytical, diagnostic and therapeutic context of ECs0673


  1. Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Den Blaauwen, T., Aarsman, M.E., Vischer, N.O., Nanninga, N. Mol. Microbiol. (2003) [Pubmed]
  2. Nucleotide sequences of the pbpX genes encoding the penicillin-binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506. Laible, G., Hakenbeck, R., Sicard, M.A., Joris, B., Ghuysen, J.M. Mol. Microbiol. (1989) [Pubmed]
  3. Molecular cloning of the gene of a penicillin-binding protein supposed to cause high resistance to beta-lactam antibiotics in Staphylococcus aureus. Matsuhashi, M., Song, M.D., Ishino, F., Wachi, M., Doi, M., Inoue, M., Ubukata, K., Yamashita, N., Konno, M. J. Bacteriol. (1986) [Pubmed]
  4. Penicillin-binding proteins from Erwinia amylovora: mutants lacking PBP2 are avirulent. Milner, J.S., Dymock, D., Cooper, R.M., Roberts, I.S. J. Bacteriol. (1993) [Pubmed]
  5. Effects of furazlocillin, a beta-lactam antibiotic which binds selectively to penicillin-binding protein 3, on Escherichia coli mutants deficient in other penicillin-binding proteins. Schmidt, L.S., Botta, G., Park, J.T. J. Bacteriol. (1981) [Pubmed]
  6. Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein. Ishino, F., Park, W., Tomioka, S., Tamaki, S., Takase, I., Kunugita, K., Matsuzawa, H., Asoh, S., Ohta, T., Spratt, B.G. J. Biol. Chem. (1986) [Pubmed]
  7. Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli. Navarro, F., Robin, A., D'Ari, R., Joseleau-Petit, D. Mol. Microbiol. (1998) [Pubmed]
  8. Interactions of Yersinia pestis penicillin-binding proteins with beta-lactam antibiotics. Ferreira, R.C., Park, J.T., Camelo, D., De Almeida, D.F., Ferreira, L.C. Antimicrob. Agents Chemother. (1995) [Pubmed]
  9. Involvement of penicillin-binding protein 2 with other penicillin-binding proteins in lysis of Escherichia coli by some beta-lactam antibiotics alone and in synergistic lytic effect of amdinocillin (mecillinam). Gutmann, L., Vincent, S., Billot-Klein, D., Acar, J.F., Mrèna, E., Williamson, R. Antimicrob. Agents Chemother. (1986) [Pubmed]
  10. Comparison of cefepime, cefpirome, and cefaclidine binding affinities for penicillin-binding proteins in Escherichia coli K-12 and Pseudomonas aeruginosa SC8329. Pucci, M.J., Boice-Sowek, J., Kessler, R.E., Dougherty, T.J. Antimicrob. Agents Chemother. (1991) [Pubmed]
  11. Target for bacteriostatic and bactericidal activities of beta-lactam antibiotics against Escherichia coli resides in different penicillin-binding proteins. Satta, G., Cornaglia, G., Mazzariol, A., Golini, G., Valisena, S., Fontana, R. Antimicrob. Agents Chemother. (1995) [Pubmed]
  12. Diffusion of meropenem and imipenem through the outer membrane of Escherichia coli K-12 and correlation with their antibacterial activities. Cornaglia, G., Guan, L., Fontana, R., Satta, G. Antimicrob. Agents Chemother. (1992) [Pubmed]
  13. Possible physiological functions of penicillin-binding proteins in Staphylococcus aureus. Georgopapadakou, N.H., Dix, B.A., Mauriz, Y.R. Antimicrob. Agents Chemother. (1986) [Pubmed]
  14. The Staphylococcus aureus mec determinant comprises an unusual cluster of direct repeats and codes for a gene product similar to the Escherichia coli sn-glycerophosphoryl diester phosphodiesterase. Ryffel, C., Bucher, R., Kayser, F.H., Berger-Bächi, B. J. Bacteriol. (1991) [Pubmed]
  15. Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin-binding protein 2 of Escherichia coli K12. Asoh, S., Matsuzawa, H., Ishino, F., Strominger, J.L., Matsuhashi, M., Ohta, T. Eur. J. Biochem. (1986) [Pubmed]
  16. Moxalactam (6059-S), a new 1-oxa-beta-lactam: binding affinity for penicillin-binding proteins of Escherichia coli K-12. Komatsu, Y., Nishikawa, T. Antimicrob. Agents Chemother. (1980) [Pubmed]
  17. Affinity of temocillin for Escherichia coli K-12 penicillin-binding proteins. Labia, R., Baron, P., Masson, J.M., Hill, G., Cole, M. Antimicrob. Agents Chemother. (1984) [Pubmed]
  18. Penicillin-binding protein 1 of Staphylococcus aureus is essential for growth. Wada, A., Watanabe, H. J. Bacteriol. (1998) [Pubmed]
  19. A water-soluble form of penicillin-binding protein 2 of Escherichia coli constructed by site-directed mutagenesis. Adachi, H., Ohta, T., Matsuzawa, H. FEBS Lett. (1987) [Pubmed]
  20. Potent activity of meropenem against Escherichia coli arising from its simultaneous binding to penicillin-binding proteins 2 and 3. Sumita, Y., Fukasawa, M. J. Antimicrob. Chemother. (1995) [Pubmed]
  21. Morphology of an Escherichia coli mutant with a temperature-dependent round cell shape. Iwaya, M., Goldman, R., Tipper, D.J., Feingold, B., Strominger, J.L. J. Bacteriol. (1978) [Pubmed]
  22. GNA33 from Neisseria meningitidis serogroup B encodes a membrane-bound lytic transglycosylase (MltA). Jennings, G.T., Savino, S., Marchetti, E., Aricò, B., Kast, T., Baldi, L., Ursinus, A., Höltje, J.V., Nicholas, R.A., Rappuoli, R., Grandi, G. Eur. J. Biochem. (2002) [Pubmed]
  23. On the role of the high molecular weight penicillin-binding proteins in the cell cycle of Escherichia coli. Wientjes, F.B., Nanninga, N. Res. Microbiol. (1991) [Pubmed]
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