ArticleMicrobial drug resistance (Larchmont, N.Y.)2014
Penicillin-binding protein 2x of Streptococcus pneumoniae: the mutation Ala707Asp within the C-terminal PASTA2 domain leads to destabilization.
Article in Microbial drug resistance (Larchmont, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Zinc Oxide Quantum Dots May Provide a Novel Potential Treatment for Antibiotic-ResistantMolecules (Basel, Switzerland) · 2023Article
- New Insights into Beta-Lactam Resistance ofMicroorganisms · 2021Article
- Review
- The Role of Cadaverine Synthesis on Pneumococcal Capsule and Protein Expression.Medical sciences (Basel, Switzerland) · 2018Article
- Promoter Identification and Transcription Analysis of Penicillin-Binding Protein Genes in Streptococcus pneumoniae R6.Microbial drug resistance (Larchmont, N.Y.) · 2016Article
- Distribution of PASTA domains in penicillin-binding proteins and serine/threonine kinases of Actinobacteria.The Journal of antibiotics · 2016Review
- Glycosyltransferases and Transpeptidases/Penicillin-Binding Proteins: Valuable Targets for New Antibacterials.Antibiotics (Basel, Switzerland) · 2016Review
- Profiling of β-lactam selectivity for penicillin-binding proteins in Streptococcus pneumoniae D39.Antimicrobial agents and chemotherapy · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus pneumoniae penicillin-binding protein 2x (PBP2x) is an enzyme involved in the last stages of peptidoglycan assembly and essential for bacterial growth and survival. PBP2x localizes to the division site, a process that depends on its Penicillin-Binding Protein And Serine-Threonine-kinase Associated (PASTA) domains, which was previously demonstrated via GFP-PBP2x in living cells. During this study a mutant strain was isolated in which the GFP-PBP2x fusion protein did not localize at division sites and it contained reduced amounts of the full-length GFP-PBP2x. We now show that this defect is due to a point mutation within the C-terminal PASTA2 domain of PBP2x. The mutant protein was analyzed in detail in terms of beta-lactam binding, functionality, and localization in live cells. We demonstrate that the mutation affects the GFP-tagged PBP2x variant severely and renders it susceptible to the protease/chaperone HtrA.
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