ArticlePLoS pathogens2011
A structural model for binding of the serine-rich repeat adhesin GspB to host carbohydrate receptors.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 85 citations in OpenAlex.
- Oral streptococci utilize a Siglec-like domain of serine-rich repeat adhesins to preferentially target platelet sialoglycans in human blood.PLoS pathogens · 2014Trial
- Identification of interbacterial adhesion between oral Schaalia species and streptococcal serine-rich repeat glycoproteins.FEMS microbiology letters · 2026Article
- Structural Basis for how Sialoglycan-binding Viridans Streptococci Accommodate Ligands that Exceed the Characterized Binding Site.microPublication biology · 2026Article
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- Crystal structure of the long Rib domain of the LPXTG-anchored surface protein from Limosilactobacillus reuteri.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Molecular Insights into O-Linked Sialoglycans Recognition by the Siglec-Like SLBR-N (SLBRACS central science · 2024Article
- Glycoproteomic landscape and structural dynamics of TIM family immune checkpoints enabled by mucinase SmE.Nature communications · 2023Article
- TapA acts as specific chaperone in TasA filament formation by strand complementation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- SssP1, a Fimbria-like component of Streptococcus suis, binds to the vimentin of host cells and contributes to bacterial meningitis.PLoS pathogens · 2022Article
- Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.Nature communications · 2022Article
- Article
- Proteoglycan 4 (lubricin) is a highly sialylated glycoprotein associated with cardiac valve damage in animal models of infective endocarditis.Glycobiology · 2021Article
- Molecular recognition of sialoglycans by streptococcal Siglec-like adhesins: toward the shape of specific inhibitors.RSC chemical biology · 2021Article
- A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of Infective endocarditis.PLoS pathogens · 2021Article
- Tandem sialoglycan-binding modules in aThe Journal of biological chemistry · 2020Article
- Structure based virtual screening identifies small molecule effectors for the sialoglycan binding protein Hsa.The Biochemical journal · 2020Article
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- Streptococcus oralis subsp.Infection and immunity · 2019Article
- Recognition of specific sialoglycan structures by oral streptococci impacts the severity of endocardial infection.PLoS pathogens · 2019Article
- The Two Distinct Types of SecA2-Dependent Export Systems.Microbiology spectrum · 2019Review
Corrections and comments
- Erratum issued
Authors and funding
13 authors at 6 institutions in 1 country.
Funding
Abstract
GspB is a serine-rich repeat (SRR) adhesin of Streptococcus gordonii that mediates binding of this organism to human platelets via its interaction with sialyl-T antigen on the receptor GPIbα. This interaction appears to be a major virulence determinant in the pathogenesis of infective endocarditis. To address the mechanism by which GspB recognizes its carbohydrate ligand, we determined the high-resolution x-ray crystal structure of the GspB binding region (GspB(BR)), both alone and in complex with a disaccharide precursor to sialyl-T antigen. Analysis of the GspB(BR) structure revealed that it is comprised of three independently folded subdomains or modules: 1) an Ig-fold resembling a CnaA domain from prokaryotic pathogens; 2) a second Ig-fold resembling the binding region of mammalian Siglecs; 3) a subdomain of unique fold. The disaccharide was found to bind in a pocket within the Siglec subdomain, but at a site distinct from that observed in mammalian Siglecs. Confirming the biological relevance of this binding pocket, we produced three isogenic variants of S. gordonii, each containing a single point mutation of a residue lining this binding pocket. These variants have reduced binding to carbohydrates of GPIbα. Further examination of purified GspB(BR)-R484E showed reduced binding to sialyl-T antigen while S. gordonii harboring this mutation did not efficiently bind platelets and showed a significant reduction in virulence, as measured by an animal model of endocarditis. Analysis of other SRR proteins revealed that the predicted binding regions of these adhesins also had a modular organization, with those known to bind carbohydrate receptors having modules homologous to the Siglec and Unique subdomains of GspB(BR). This suggests that the binding specificity of the SRR family of adhesins is determined by the type and organization of discrete modules within the binding domains, which may affect the tropism of organisms for different tissues.
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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.