Literature DB >> 2722720

Interaction of cephalosporins with penicillin-binding proteins of methicillin-resistant Staphylococcus aureus.

S E Truesdell1, G E Zurenko, A L Laborde.   

Abstract

The binding affinity of cefmetazole for penicillin binding proteins (PBPs) of methicillin resistant Staphylococcus aureus (MRSA) was compared with the affinities of cefazolin, cefotetan, and cefoxitin for these same sites. Overall, cefmetazole was found to have comparable or higher affinity for PBP1, PBP2, and PBP3 than cefoxitin or cefotetan; its affinity for these PBPs is lower than that of cefazolin. Interestingly, the antibiotic showed a somewhat greater affinity for PBP2' (PBP2a) than cefazolin, cefotetan, and cefoxitin. These results suggest that the somewhat lower MICs detected with cefmetazole for MRSA may be a consequence of the interaction of the antibiotic with PBP2'.

Entities:  

Mesh:

Substances:

Year:  1989        PMID: 2722720     DOI: 10.1093/jac/23.suppl_d.13

Source DB:  PubMed          Journal:  J Antimicrob Chemother        ISSN: 0305-7453            Impact factor:   5.790


  1 in total

1.  In vitro antibacterial activity and interactions with beta-lactamases and penicillin-binding proteins of the new monocarbam antibiotic U-78608.

Authors:  G E Zurenko; S E Truesdell; B H Yagi; R J Mourey; A L Laborde
Journal:  Antimicrob Agents Chemother       Date:  1990-05       Impact factor: 5.191

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.