Effect of a beta-lactamase inhibitor, tazobactam, on growth and penicillin-binding proteins of Borrelia burgdorferi. Academic Article uri icon

Overview

abstract

  • The effects of tazobactam, a relatively new beta-lactamase inhibitor, were investigated on growth and penicillin-binding proteins (PBPs) of Borrellia burgdorferi. A previous communication from our group demonstrated several proteins capable of binding labelled penicillin in this organism. Of these proteins, 94-kDa and 57-kDa PBPs possessed the highest affinity for penicillin and were assumed to be essential proteins involved in cell-wall synthesis. In these experiments, tazobactam was used in competition binding experiments as well as on whole spirochetes. Only the 94-kDa and 57-kDa PBPs were affected by increasing amounts of tazobactam during competition-binding experiments and growth of B. burgdorferi was also inhibited. These results may explain the in vitro activity of beta-lactamase inhibitors in general and suggest a utility for these compounds when examining PBPs with hydrolysing activity and/or organisms with beta-lactamases.

publication date

  • July 15, 1991

Research

keywords

  • Bacterial Proteins
  • Borrelia burgdorferi Group
  • Hexosyltransferases
  • Penicillanic Acid
  • Peptidyl Transferases

Identity

Scopus Document Identifier

  • 0025886220

Digital Object Identifier (DOI)

  • 10.1016/0378-1097(91)90430-i

PubMed ID

  • 1657694

Additional Document Info

volume

  • 66

issue

  • 1