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Gene Review:

pbpA - penicillin-binding protein 2

Pseudomonas aeruginosa PAO1

Neu, H.C., Sumita, Y. et al., García-de los Santos, A. et al., Fung-Tomc, J.C. et al.

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Disease relevance of pbpA

In Rhizobium etli CFN42, both the symbiotic plasmid (pd) and plasmid b (pb) are required for effective bean nodulation [1].

High impact information on pbpA

Binding of penicillins to penicillin-binding protein 1Bs produces lysis, binding to penicillin-binding protein 2 produces round cells, and binding to penicillin-binding protein 3 produces long filaments [2].
Amdinocillin is a beta-amidino penicillanic acid derivative that binds specifically to penicillin-binding protein 2 [2].
Compared with imipenem and meropenem, BMS-181139 may have a slightly higher affinity for penicillin-binding protein 2 (PBP-2) of P. aeruginosa [3].
SM-17466, at a 50% inhibitory concentration of less than 1 microgram/ml, bound to penicillin-binding proteins 1 to 4 in methicillin-susceptible S. aureus and also had good binding to penicillin-binding protein 2' in a methicillin-resistant strain (50% inhibitory concentration, 5.9 micrograms/ml) [4].
This is due to the presence on pb of a region (lps beta) involved in lipopolysaccharide (LPS) biosynthesis [1].

References

Characterization of two plasmid-borne lps beta loci of Rhizobium etli required for lipopolysaccharide synthesis and for optimal interaction with plants. García-de los Santos, A., Brom, S. Mol. Plant Microbe Interact. (1997) [Pubmed]
Penicillin-binding proteins and role of amdinocillin in causing bacterial cell death. Neu, H.C. Am. J. Med. (1983) [Pubmed]
Activity of carbapenem BMS-181139 against Pseudomonas aeruginosa is not dependent on porin protein D2. Fung-Tomc, J.C., Gradelski, E., Kolek, B., Minassian, B., Pucci, M., Kessler, R.E., Bonner, D.P. Antimicrob. Agents Chemother. (1995) [Pubmed]
Antimicrobial activity of SM-17466, a novel carbapenem antibiotic with potent activity against methicillin-resistant Staphylococcus aureus. Sumita, Y., Nouda, H., Kanazawa, K., Fukasawa, M. Antimicrob. Agents Chemother. (1995) [Pubmed]

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