BRO beta-lactamases of Branhamella catarrhalis and Moraxella subgenus Moraxella, including evidence for chromosomal beta-lactamase transfer by conjugation in B. catarrhalis, M. nonliquefaciens, and M. lacunata

Antimicrob Agents Chemother. 1989 Nov;33(11):1845-54. doi: 10.1128/AAC.33.11.1845.

Abstract

Two closely related beta-lactamases, BRO-1 and BRO-2 (formerly called Ravasio and 1908), are found in Moraxella (Branhamella) catarrhalis. We screened strains of B. catarrhalis recovered in the United States since 1952 and identified the first beta-lactamase-positive isolate in August 1976. The prevalence of the enzymes among 394 clinical isolates from one Texas hospital has averaged 75% since testing began in 1983. Screening of isolates of Moraxella subgenus Moraxella revealed the BRO enzymes in two other human respiratory tract species, M. lacunata and M. nonliquefaciens, beginning in 1978. A different beta-lactamase with a pI of 6.4 predominated in other species of subgenus Moraxella. BRO-2 had a different isoelectric focusing pattern and was produced in lesser amounts than BRO-1, but the two enzymes were indistinguishable by substrate or inhibitor profile. BRO enzymes from B. catarrhalis, M. nonliquefaciens, and M. lacunata could be transferred by conjugation and, for B. catarrhalis, also by transformation to B. catarrhalis. Plasmid bands were demonstrated in 90% of M. nonliquefaciens and in one previously reported strain of B. catarrhalis, but no change in plasmid profiles was seen in beta-lactamase-positive recombinants, supporting previous studies that suggested the beta-lactamase genes are chromosomal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromosomes, Bacterial
  • Conjugation, Genetic
  • DNA, Bacterial / genetics
  • Kinetics
  • Moraxella / enzymology*
  • Moraxella / genetics
  • Moraxella catarrhalis / enzymology*
  • Moraxella catarrhalis / genetics
  • Plasmids
  • Substrate Specificity
  • Transformation, Bacterial
  • beta-Lactamase Inhibitors
  • beta-Lactamases / metabolism*

Substances

  • DNA, Bacterial
  • beta-Lactamase Inhibitors
  • beta-Lactamases