Browse AMR Mutations
Explore antimicrobial resistance mutations from the literature
Explore antimicrobial resistance mutations from the literature
Overview
All detectable high-molecular-mass penicillin-binding proteins are modified in a high-level beta-lactam-resistant clinical isolate of Streptococcus mitis.
The resistant strain 127R shows T446A and A619G changes in the transpeptidase domain.
Highly variable penicillin resistance determinants PBP 2x, PBP 2b, and PBP 1a in isolates of two Streptococcus pneumoniae clonal groups, Poland 23F-16 and Poland 6B-20.
Biochemical characterization of Streptococcus pneumoniae penicillin-binding protein 2b and Its implication in beta-lactam resistance.
The Thr446Ala mutation is always observed in CR strains and is close to the key conserved motif (S 443 SN). The Thr446Ala mutation in R6 PBP2b* displays a 60% reduction in penicillin G affinity in vitro compared to that for the wild-type protein. A recombinant R6 strain expressing the R6 PBP2b Thr446Ala mutation is twofold less sensitive to piperacillin than the parental S. pneumoniae strain.
Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance.
Mutations T446A, E476G, and T489S in PBP 2b are associated with reduced susceptibility to penicillin G and cefotaxime.
Commensal streptococci serve as a reservoir for β-lactam resistance genes in Streptococcus pneumoniae.
Mutations in pbp2b are associated with reduced susceptibility to beta-lactam antibiotics.
Prevalence and resistance characteristics of multidrug-resistant Streptococcus pneumoniae isolated from the respiratory tracts of hospitalized children in Shenzhen, China.
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