ArticleAntimicrobial agents and chemotherapy2001
All detectable high-molecular-mass penicillin-binding proteins are modified in a high-level beta-lactam-resistant clinical isolate of Streptococcus mitis.
Article in Antimicrobial agents and chemotherapy, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Group A streptococcus isolated in Guyana with reduced susceptibility to β-lactam antibiotics.Access microbiology · 2024Article
- Article
- Commensal streptococci serve as a reservoir for β-lactam resistance genes in Streptococcus pneumoniae.Antimicrobial agents and chemotherapy · 2015Article
- Identification of clinically relevant viridans group streptococci by phenotypic and genotypic analysis.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2011Article
- Problems in monitoring horizontal gene transfer in field trials of transgenic plants.Nature biotechnology · 2004Article
- Complete sequences of six penicillin-binding protein genes from 40 Streptococcus pneumoniae clinical isolates collected in Japan.Antimicrobial agents and chemotherapy · 2004Article
- Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.Microbiology and molecular biology reviews : MMBR · 2002Review
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All detectable high-molecular-mass penicillin-binding proteins (HMM PBPs) are altered in a clinical isolate of Streptococcus mitis for which the beta-lactam MICs are increased from those previously reported in our region (cefotaxime MIC, 64 microg/ml). These proteins were hardly detected at concentrations that saturate all PBPs in clinical isolates and showed, after densitometric analysis, 50-fold-lower radiotracer binding. Resistance was related to mosaic structure in all HMM PBP-coding genes, where critical region replacement was complemented not only by substitutions already reported for the closely related Streptococcus pneumoniae but also by other specific replacements that are presumably close to the active-site serine. Mosaic structure was also presumed in a pbp1a-sensitive strain used for comparison, confirming that these structures do not unambiguously imply, by themselves, detectable critical changes in the kinetic properties of these proteins.
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