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. 1990 Feb;34(2):363–365. doi: 10.1128/aac.34.2.363

Identification of a group of Haemophilus influenzae penicillin-binding proteins that may have complementary physiological roles.

F Malouin 1, T R Parr Jr 1, L E Bryan 1
PMCID: PMC171589  PMID: 2327782

Abstract

[35S]penicillin bound to different Haemophilus influenzae proteins in assays performed at 20, 37, or 42 degrees C. Penicillin-binding proteins 3a, 3b, 4, and 4' formed a group characterized by their affinity for moxalactam, cefotaxime, and piperacillin. Penicillin-binding protein 4' showed specific properties that may reflect its complementary role in septation.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Laemmli U. K., Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973 Nov 15;80(4):575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  2. Makover S. D., Wright R., Telep E. Penicillin-binding proteins in Haemophilus influenzae. Antimicrob Agents Chemother. 1981 Apr;19(4):584–588. doi: 10.1128/aac.19.4.584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Malouin F., Bryan L. E. Haemophilus influenzae penicillin-binding proteins 1a and 3 possess distinct and opposite temperature-modulated penicillin-binding activities. Antimicrob Agents Chemother. 1988 Apr;32(4):498–502. doi: 10.1128/aac.32.4.498. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Mendelman P. M., Chaffin D. O., Musser J. M., De Groot R., Serfass D. A., Selander R. K. Genetic and phenotypic diversity among ampicillin-resistant, non-beta-lactamase-producing, nontypeable Haemophilus influenzae isolates. Infect Immun. 1987 Nov;55(11):2585–2589. doi: 10.1128/iai.55.11.2585-2589.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Parr T. R., Jr, Bryan L. E. Mechanism of resistance of an ampicillin-resistant, beta-lactamase-negative clinical isolate of Haemophilus influenzae type b to beta-lactam antibiotics. Antimicrob Agents Chemother. 1984 Jun;25(6):747–753. doi: 10.1128/aac.25.6.747. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Serfass D. A., Mendelman P. M., Chaffin D. O., Needham C. A. Ampicillin resistance and penicillin-binding proteins of Haemophilus influenzae. J Gen Microbiol. 1986 Oct;132(10):2855–2861. doi: 10.1099/00221287-132-10-2855. [DOI] [PubMed] [Google Scholar]
  7. Tipper D. J. Mode of action of beta-lactam antibiotics. Pharmacol Ther. 1985;27(1):1–35. doi: 10.1016/0163-7258(85)90062-2. [DOI] [PubMed] [Google Scholar]
  8. Waxman D. J., Strominger J. L. Penicillin-binding proteins and the mechanism of action of beta-lactam antibiotics. Annu Rev Biochem. 1983;52:825–869. doi: 10.1146/annurev.bi.52.070183.004141. [DOI] [PubMed] [Google Scholar]

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