ArticleProtein science : a publication of the Protein Society2009
Crystal structure of the variable domain of the Streptococcus gordonii surface protein SspB.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- TargetingACS medicinal chemistry letters · 2026Article
- The structure ofInfection and immunity · 2026Article
- The polymicrobial pathogenicity ofFrontiers in oral health · 2024Article
- Structural foundation for the role of enterococcal PrgB in conjugation, biofilm formation, and virulence.eLife · 2023Article
- Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB.Acta crystallographica. Section D, Structural biology · 2021Article
- Collagen Binding Proteins of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture.The Journal of biological chemistry · 2020Article
- The Multifaceted Nature of Streptococcal Antigen I/II Proteins in Colonization and Disease Pathogenesis.Frontiers in microbiology · 2020Review
- Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins.Frontiers in microbiology · 2020Review
- PrgB promotes aggregation, biofilm formation, and conjugation through DNA binding and compaction.Molecular microbiology · 2018Article
- Glucan Binding Protein C of Streptococcus mutans Mediates both Sucrose-Independent and Sucrose-Dependent Adherence.Infection and immunity · 2018Article
- Surface-exposed loops and an acidic patch in the Scl1 protein of group AThe Journal of biological chemistry · 2018Article
- Coassociation between Group B Streptococcus and Candida albicans Promotes Interactions with Vaginal Epithelium.Infection and immunity · 2018Article
- The Streptococcus gordonii Adhesin CshA Protein Binds Host Fibronectin via a Catch-Clamp Mechanism.The Journal of biological chemistry · 2017Article
- Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae.The Journal of biological chemistry · 2016Article
- Multispecies biofilms and host responses: "discriminating the trees from the forest".Cytokine · 2013Review
- Structural and functional analysis of the N-terminal domain of the Streptococcus gordonii adhesin Sgo0707.PloS one · 2013Article
- Stick to your gums: mechanisms of oral microbial adherence.Journal of dental research · 2011Review
- Streptococcus pyogenes antigen I/II-family polypeptide AspA shows differential ligand-binding properties and mediates biofilm formation.Molecular microbiology · 2011Article
- Mechanism of adhesion maintenance by methionine sulphoxide reductase in Streptococcus gordonii.Molecular microbiology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The Antigen I/II (AgI/II) family of proteins are cell wall anchored adhesins expressed on the surface of oral streptococci. The AgI/II proteins interact with molecules on other bacteria, on the surface of host cells, and with salivary proteins. Streptococcus gordonii is a commensal bacterium, and one of the primary colonizers that initiate the formation of the oral biofilm. S. gordonii expresses two AgI/II proteins, SspA and SspB that are closely related. One of the domains of SspB, called the variable (V-) domain, is significantly different from corresponding domains in SspA and all other AgI/II proteins. As a first step to elucidate the differences among these proteins, we have determined the crystal structure of the V-domain from S. gordonii SspB at 2.3 A resolution. The domain comprises a beta-supersandwich with a putative binding cleft stabilized by a metal ion. The overall structure of the SspB V-domain is similar to the previously reported V-domain of the Streptococcus mutans protein SpaP, despite their low sequence similarity. In spite of the conserved architecture of the binding cleft, the cavity is significantly smaller in SspB, which may provide clues about the difference in ligand specificity. We also verified that the metal in the binding cleft is a calcium ion, in concurrence with previous biological data. It was previously suggested that AgI/II V-domains are carbohydrate binding. However, we tested that hypothesis by screening the SspB V-domain for binding to over 400 glycoconjucates and found that the domain does not interact with any of the carbohydrates.
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