ArticleAntimicrobial agents and chemotherapy2009
An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: mutational analysis of Thr338.
Article in Antimicrobial agents and chemotherapy, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 37 citations in OpenAlex.
- RelA-mediated (p)ppGpp accumulation links glucose starvation to peptidoglycan synthesis arrest and spherical morphogenesis via PBP2x and FtsX inJournal of bacteriology · 2026Article
- Machine learning-based virtual screening and density functional theory characterisation of natural inhibitors targeting mutant PBP2x in Streptococcus pneumoniae.Scientific reports · 2025Article
- Molecular Targets inGenes · 2024Review
- Fructose promotes ampicillin killing of antibiotic-resistantVirulence · 2023Article
- Amoxicillin-resistanteLife · 2022Article
- Molecular Characterization of Penicillin-Binding Protein2x, 2b and 1a ofFrontiers in microbiology · 2022Article
- New Insights into Beta-Lactam Resistance ofMicroorganisms · 2021Article
- Transformation of nonencapsulated Streptococcus pneumoniae during systemic infection.Scientific reports · 2020Article
- Raman-activated sorting of antibiotic-resistant bacteria in human gut microbiota.Environmental microbiology · 2020Article
- On Column Binding a Real-Time Biosensor forMolecules (Basel, Switzerland) · 2020Article
- New Aspects of the Interplay between Penicillin Binding Proteins,Antimicrobial agents and chemotherapy · 2017Article
- Insight into the Diversity of Penicillin-Binding Protein 2x Alleles and Mutations in Viridans Streptococci.Antimicrobial agents and chemotherapy · 2017Article
- β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.Cold Spring Harbor perspectives in medicine · 2016Review
- Pbp2x localizes separately from Pbp2b and other peptidoglycan synthesis proteins during later stages of cell division of Streptococcus pneumoniae D39.Molecular microbiology · 2014Article
- Comprehensive identification of single nucleotide polymorphisms associated with beta-lactam resistance within pneumococcal mosaic genes.PLoS genetics · 2014Article
- A low-affinity penicillin-binding protein 2x variant is required for heteroresistance in Streptococcus pneumoniae.Antimicrobial agents and chemotherapy · 2014Article
- The elongation of ovococci.Microbial drug resistance (Larchmont, N.Y.) · 2014Review
- Penicillin-binding protein 2x of Streptococcus pneumoniae: the mutation Ala707Asp within the C-terminal PASTA2 domain leads to destabilization.Microbial drug resistance (Larchmont, N.Y.) · 2014Article
- Requirement of essential Pbp2x and GpsB for septal ring closure in Streptococcus pneumoniae D39.Molecular microbiology · 2013Article
- Heteroresistance to fosfomycin is predominant in Streptococcus pneumoniae and depends on the murA1 gene.Antimicrobial agents and chemotherapy · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Penicillin-binding protein 2x (PBP2x) of Streptococcus pneumoniae represents a primary resistance determinant for beta-lactams, and low-affinity PBP2x variants can easily be selected with cefotaxime. Penicillin-resistant clinical isolates of S. pneumoniae frequently contain in their mosaic PBP2x the mutation T338A adjacent to the active site S337, and T338P as well as T338G substitutions are also known. Site-directed mutagenesis has now documented that a single point mutation at position T338 confers selectable levels of beta-lactam resistance preferentially to oxacillin. Despite the moderate impact on beta-lactam susceptibility, the function of the PBP2x mutants appears to be impaired, as can be documented in the absence of a functional CiaRH regulatory system, resulting in growth defects and morphological changes. The combination of low-affinity PBP2x and PBP1a encoded by mosaic genes is known to result in high cefotaxime resistance. In contrast, introduction of a mosaic pbp1a into the PBP2x(T338G) mutant did not lead to increased resistance. However, the mosaic PBP1a gene apparently complemented the PBP2x(T338G) defect, since Cia mutant derivatives grew normally. The data support the view that PBP2x and PBP1a interact with each other on some level and that alterations of both PBPs in resistant clinical isolates have evolved to ensure cooperation between both proteins.
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