ArticlePloS one2016
Two Arginine Residues of Streptococcus gordonii Sialic Acid-Binding Adhesin Hsa Are Essential for Interaction to Host Cell Receptors.
Article in PloS one, 2016. 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 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- A Reversible and Dynamic Surface Functionalization for Fluidity Controlled Multivalent Recognition of Lectins and Bacteria.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A comparative in silico analysis of the vlhA gene regions of Mycoplasma gallisepticum and Mycoplasma synoviae isolates from commercial hen farms in Mexico.Access microbiology · 2025Article
- Oral streptococci: modulators of health and disease.Frontiers in cellular and infection microbiology · 2024Review
- Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.Nature communications · 2022Article
- 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
- Streptococcus gordonii DL1 evades polymorphonuclear leukocyte-mediated killing via resistance to lysozyme.PloS one · 2021Article
- Review
- Tandem sialoglycan-binding modules in aThe Journal of biological chemistry · 2020Article
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- A Sensitive and Rapid Method to Determin the Adhesion Capacity of Probiotics and Pathogenic Microorganisms to Human Gastrointestinal Mucins.Microorganisms · 2018Article
- Structural basis for the role of serine-rich repeat proteins fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Serine-Rich Repeat Adhesins Contribute toFrontiers in microbiology · 2017Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsa is a large, serine-rich protein of Streptococcus gordonii DL1 that mediates binding to α2-3-linked sialic acid termini of glycoproteins, including platelet glycoprotein Ibα, and erythrocyte membrane protein glycophorin A, and band 3. The binding of Hsa to platelet glycoprotein Ibα contributes to the pathogenesis of infective endocarditis. This interaction appears to be mediated by a second non-repetitive region (NR2) of Hsa. However, the molecular details of the interaction between the Hsa NR2 region and these glycoproteins are not well understood. In the present study, we identified the amino acid residues of the Hsa NR2 region that are involved in sialic acid recognition. To identify the sialic acid-binding site of Hsa NR2 region, we prepared various mutants of Hsa NR2 fused with glutathione transferase. Fusion proteins harboring Arg340 to Asn (R340N) or Arg365 to Asn (R365N) substitutions in the NR2 domain exhibited significantly reduced binding to human erythrocytes and platelets. A sugar-binding assay showed that these mutant proteins abolished binding to α2-3-linked sialic acid. Furthermore, we established S. gordonii DL1 derivatives that encoded the corresponding Hsa mutant protein. In whole-cell assays, these mutant strains showed significant reductions in hemagglutination, in platelet aggregation, and in adhesion to human leukocytes. These results indicate that the Arg340 and Arg365 residues of Hsa play an important role in the binding of Hsa to α2-3-linked sialic acid-containing glycoproteins.
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