Abstract
Beta-lactam resistance poses a major problem in the chemotherapy of shigellosis caused byShigella dysenteriae.Such resistance may arise from alterations in the affinities or amounts of the penicillin-binding proteins (PBPs) for beta-lactams, elaboration of beta-lactamases and reduced permeability across the outer membrane. The mechanisms of resistance inS. dysenteriaehave not been studied in depth. This report describes a laboratory mutant, M19 which was characterized by the appearance of two high molecular mass PBPs of 84 (PBP1′) and 82 kDa (PBP1″). M19 was more resistant to cefsulodin and cefoxitin. Resistance could be correlated with lower second order rate constants (k+2/K) of acylation. Moreover there was an overall two-fold increase in the relative amount of PBP1 (i.e. 1′+1″) in the mutant M19 compared to C152. This is the first report which presents evidence of the involvement of altered high molecular mass PBPs in beta-lactam resistance inS. dysenteriae.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
