ArticleScientific reports2016
Modular Architecture and Unique Teichoic Acid Recognition Features of Choline-Binding Protein L (CbpL) Contributing to Pneumococcal Pathogenesis.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Lipidation of pneumococcal proteins enables activation of human antigen-presenting cells and initiation of an adaptive immune response.Frontiers in immunology · 2024Article
- Investigation of choline-binding protein of CbpD in the pathogenesis ofFrontiers in veterinary science · 2024Article
- Role of cell surface proteins and toll-like receptors in the pathogenesis ofIranian journal of basic medical sciences · 2024Article
- The choline-binding proteins PspA, PspC, and LytA ofInfection and immunity · 2023Article
- Review
- A Jack of All Trades: The Role of Pneumococcal Surface Protein A in the Pathogenesis ofFrontiers in cellular and infection microbiology · 2022Review
- The Two-Component System 09 ofMicroorganisms · 2021Article
- Streptococcus pneumoniae hijacks host autophagy by deploying CbpC as a decoy for Atg14 depletion.EMBO reports · 2020Article
- The Versatility of Opportunistic Infections Caused byFrontiers in microbiology · 2020Article
- Article
- Article
- Identification of evolutionarily conserved virulence factor by selective pressure analysis ofCommunications biology · 2019Article
- Streptococcus pneumoniae: transmission, colonization and invasion.Nature reviews. Microbiology · 2018Review
- Lipoteichoic acid deficiency permits normal growth but impairs virulence of Streptococcus pneumoniae.Nature communications · 2017Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human pathogen Streptococcus pneumoniae is decorated with a special class of surface-proteins known as choline-binding proteins (CBPs) attached to phosphorylcholine (PCho) moieties from cell-wall teichoic acids. By a combination of X-ray crystallography, NMR, molecular dynamics techniques and in vivo virulence and phagocytosis studies, we provide structural information of choline-binding protein L (CbpL) and demonstrate its impact on pneumococcal pathogenesis and immune evasion. CbpL is a very elongated three-module protein composed of (i) an Excalibur Ca
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