ArticleInfection and immunity2006
Penicillin-binding protein 1a promotes resistance of group B streptococcus to antimicrobial peptides.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- Antimicrobial Peptides Against Antimicrobial-Resistant Bacteria: Focus on Machine Learning.Infection and drug resistance · 2026Review
- Penicillin-Binding Proteins inAntibiotics (Basel, Switzerland) · 2026Review
- Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation.Antibiotics (Basel, Switzerland) · 2024Review
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- An opportunistic pathogen under stress: how Group B Streptococcus responds to cytotoxic reactive species and conditions of metal ion imbalance to survive.FEMS microbiology reviews · 2024Review
- Macrophage polarization duringFrontiers in microbiology · 2023Article
- The PI3K-Akt pathway is a multifaceted regulator of the macrophage response to diverse group BFrontiers in cellular and infection microbiology · 2023Article
- Multilocus sequence type-dependent activity of human and animal cathelicidins against community-, hospital-, and livestock-associated methicillin-resistantJournal of animal science and technology · 2022Article
- Identification and Characterization of Marine Microorganisms by Tandem Mass Spectrometry Proteotyping.Microorganisms · 2022Article
- Using Knock-Out Mutants to Investigate the Adhesion ofInternational journal of molecular sciences · 2021Article
- Functional Insights into the High-Molecular-Mass Penicillin-Binding Proteins of Streptococcus agalactiae Revealed by Gene Deletion and Transposon Mutagenesis Analysis.Journal of bacteriology · 2021Article
- Genome-Wide Assessment of Streptococcus agalactiae Genes Required for Survival in Human Whole Blood and Plasma.Infection and immunity · 2020Article
- Host Cathelicidin Exacerbates Group BmSphere · 2020Article
- Proteomic Adaptation ofMicroorganisms · 2020Article
- Resistance Mechanisms to Antimicrobial Peptides in Gram-Positive Bacteria.Frontiers in microbiology · 2020Review
- Avibactam Sensitizes Carbapenem-Resistant NDM-1-Producing Klebsiella pneumoniae to Innate Immune Clearance.The Journal of infectious diseases · 2019Article
- Intrinsic Maturational Neonatal Immune Deficiencies and Susceptibility to Group B Streptococcus Infection.Clinical microbiology reviews · 2017Review
- Differing mechanisms of surviving phagosomal stress among group B Streptococcus strains of varying genotypes.Virulence · 2017Article
- Comprehensive Proteomic and Metabolomic Signatures of Nontypeable Haemophilus influenzae-Induced Acute Otitis Media Reveal Bacterial Aerobic Respiration in an Immunosuppressed Environment.Molecular & cellular proteomics : MCP · 2016Article
- Bacterial Evasion of Host Antimicrobial Peptide Defenses.Microbiology spectrum · 2016Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Evasion of host immune defenses is critical for the progression of invasive infections caused by the leading neonatal pathogen, group B streptococcus (GBS). Upon characterizing the factors required for virulence in a neonatal rat sepsis model, we found that a surface-associated penicillin-binding protein (PBP1a), encoded by ponA, played an essential role in resistance of GBS to phagocytic clearance. In order to elucidate how PBP1a promotes resistance to innate immunity, we compared the susceptibility of wild-type GBS and an isogenic ponA mutant to the bactericidal components of human neutrophils. The isogenic strains were found to be equally capable of blocking complement activation on the bacterial surface and equally associated with phagocytes and susceptible to oxidative killing. In contrast, the ponA mutant was significantly more susceptible to killing by cationic antimicrobial peptides (AMPs) of the cathelicidin and defensin families, which are now recognized as integral components of innate host defense against invasive bacterial infection. These observations may help explain the sensitivity to phagocytic killing and attenuated virulence of the ponA mutant. This novel function for PBP1a in promoting resistance of GBS to AMP did not involve an alteration in bacterial surface charge or peptidoglycan cross-linking. While the peptidoglycan polymerization and cross-linking activity of PBPs are essential for bacterial survival, our study is the first to identify a role for a PBP in resistance to host AMPs.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.