ArticleAntimicrobial agents and chemotherapy2006
Mutations in penicillin-binding protein (PBP) genes and in non-PBP genes during selection of penicillin-resistant Streptococcus gordonii.
Article in Antimicrobial agents and chemotherapy, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 25 citations in OpenAlex.
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- Pharmaceutical Approaches on Antimicrobial Resistance: Prospects and Challenges.Antibiotics (Basel, Switzerland) · 2021Review
- Drug resistance of oral bacteria to new antibacterial dental monomer dimethylaminohexadecyl methacrylate.Scientific reports · 2018Article
- Substitution of Alanine at Position 184 with Glutamic Acid in Escherichia coli PBP5 Ω-Like Loop Introduces a Moderate Cephalosporinase Activity.The protein journal · 2018Article
- Hands-On Assembly of DNA Sequencing Reads as a Gateway to Bioinformatics.Journal of microbiology & biology education · 2017Article
- Strain Dependent Genetic Networks for Antibiotic-Sensitivity in a Bacterial Pathogen with a Large Pan-Genome.PLoS pathogens · 2016Article
- A low-affinity penicillin-binding protein 2x variant is required for heteroresistance in Streptococcus pneumoniae.Antimicrobial agents and chemotherapy · 2014Article
- Penicillin-binding protein gene alterations in Streptococcus uberis isolates presenting decreased susceptibility to penicillin.Antimicrobial agents and chemotherapy · 2010Article
- An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: mutational analysis of Thr338.Antimicrobial agents and chemotherapy · 2009Article
- Fitness cost and impaired survival in penicillin-resistant Streptococcus gordonii isolates selected in the laboratory.Antimicrobial agents and chemotherapy · 2008Article
- Heteroresistance to penicillin in Streptococcus pneumoniae.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Promoter and transcription analysis of penicillin-binding protein genes in Streptococcus gordonii.Antimicrobial agents and chemotherapy · 2007Article
- Mutational analysis of class A and class B penicillin-binding proteins in Streptococcus gordonii.Antimicrobial agents and chemotherapy · 2006Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Penicillin resistance in Streptococcus spp. involves multiple mutations in both penicillin-binding proteins (PBPs) and non-PBP genes. Here, we studied the development of penicillin resistance in the oral commensal Streptococcus gordonii. Cyclic exposure of bacteria to twofold-increasing penicillin concentrations selected for a progressive 250- to 500-fold MIC increase (from 0.008 to between 2 and 4 microg/ml). The major MIC increase (> or = 35-fold) was related to non-PBP mutations, whereas PBP mutations accounted only for a 4- to 8-fold additional increase. PBP mutations occurred in class B PBPs 2X and 2B, which carry a transpeptidase domain, but not in class A PBP 1A, 1B, or 2A, which carry an additional transglycosylase domain. Therefore, we tested whether inactivation of class A PBPs affected resistance development in spite of the absence of mutations. Deletion of PBP 1A or 2A profoundly slowed down resistance development but only moderately affected resistance in already highly resistant mutants (MIC = 2 to 4 microg/ml). Thus, class A PBPs might facilitate early development of resistance by stabilizing penicillin-altered peptidoglycan via transglycosylation, whereas they might be less indispensable in highly resistant mutants which have reestablished a penicillin-insensitive cell wall-building machinery. The contribution of PBP and non-PBP mutations alone could be individualized in DNA transformation. Both PBP and non-PBP mutations conferred some level of intrinsic resistance, but combining the mutations synergized them to ensure high-level resistance (> or = 2 microg/ml). The results underline the complexity of penicillin resistance development and suggest that inhibition of transglycosylase might be an as yet underestimated way to interfere with early resistance development.
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