Plasmid regulation and temperature-sensitive behavior of the Yersinia pestis penicillin-binding proteins.
AUTOR(ES)
Ferreira, R C
RESUMO
Six major bands corresponding to penicillin-binding proteins (PBPs) with molecular weights ranging from 43,000 to 97,000 were detected in cell envelopes of Yersinia pestis EV76 grown at 28 degrees C. When cells were transferred to 37 degrees C and incubated for extended periods of time, the amounts of all PBPs, except for PBP2, were gradually reduced in cell envelopes of a strain carrying a 75-kb virulence-associated plasmid (as measured by penicillin-binding capacity), whereas in a strain cured of the plasmid, all PBPs were stable. The results indicated that the stability and/or the expression of Y. pestis PBPs is affected by a temperature-inducible pathway associated with the virulence-associated plasmid.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=186525Documentos Relacionados
- Temperature-Sensitive Cell Division Mutants of Escherichia coli with Thermolabile Penicillin-Binding Proteins
- Interactions of Yersinia pestis penicillin-binding proteins with beta-lactam antibiotics.
- Identification of Treponema pallidum penicillin-binding proteins.
- Affinity of cefoperazone for penicillin-binding proteins.
- Streptococcus faecium mutants that are temperature sensitive for cell growth and show alterations in penicillin-binding proteins.