ArticleThe Journal of biological chemistry2013
Molecular mechanism by which surface antigen HP0197 mediates host cell attachment in the pathogenic bacteria Streptococcus suis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Population Genetic Architecture of theVeterinary sciences · 2026Article
- Development of a Universal Multi-Epitope Vaccine Candidate againstVeterinary sciences · 2023Article
- Comparative transcriptomic analysis reveal genes involved in the pathogenicity increase ofVirulence · 2022Article
- Streptococcus pneumoniae G5 domains bind different ligands.Protein science : a publication of the Protein Society · 2019Article
- Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium.PloS one · 2017Article
- Mechanisms of Host-Pathogen Protein Complex Formation and Bacterial Immune Evasion of Streptococcus suis Protein Fhb.The Journal of biological chemistry · 2016Article
- The CodY regulator is essential for virulence in Streptococcus suis serotype 2.Scientific reports · 2016Article
- A hypothetical model of host-pathogen interaction of Streptococcus suis in the gastro-intestinal tract.Gut microbes · 2016Review
- Streptococcus suis infection: an emerging/reemerging challenge of bacterial infectious diseases?Virulence · 2014Review
- The β-galactosidase (BgaC) of the zoonotic pathogen Streptococcus suis is a surface protein without the involvement of bacterial virulence.Scientific reports · 2014Article
- Bacterial Adhesion of Streptococcus suis to Host Cells and Its Inhibition by Carbohydrate Ligands.Biology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus suis, one of the most important and prevalent pathogens in swine, presents a major challenge to global public health. HP0197 is an S. suis surface antigen that was previously identified by immunoproteomics and can bind to the host cell surface. Here, we investigated the interaction between HP0197 and the host cell surface glycosaminoglycans (GAGs) using indirect immunofluorescence and cell adhesion inhibition assays. In addition, we determined that a novel 18-kDa domain in the N-terminal region of HP0197 functions as the GAG-binding domain. We then solved the three-dimensional structures of the N-terminal 18-kDa and C-terminal G5 domains using x-ray crystallography. Based on this structural information, the GAG-binding sites in HP0197 were predicted and subsequently verified using site-directed mutagenesis and indirect immunofluorescence. The results indicate that the positively charged residues on the exposed surface of the 18-kDa domain, which are primarily lysines, likely play a critical role in the HP0197-heparin interaction that mediates bacterium-host cell adhesion. Understanding this molecular mechanism may provide a basis for the development of effective drugs and therapeutic strategies for treating streptococcal infections.
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