ArticlePathogens (Basel, Switzerland)2016
Recruitment of Factor H to the Streptococcus suis Cell Surface is Multifactorial.
Article in Pathogens (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.
- Identification ofVirulence · 2021Pooled it
- Innate immune response to Streptococcus suis infection: advances and future challenges.Veterinary research · 2026Review
- Identification and characterization of ugpE associated with the full virulence of Streptococcus suis.Veterinary research · 2025Article
- Comparative analysis of the interactions of different Streptococcus suis strains with monocytes, granulocytes and the complement system in porcine blood.Veterinary research · 2024Article
- Immunoglobulin M-degrading enzyme ofFrontiers in immunology · 2023Article
- Neutrophils inMicroorganisms · 2021Review
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- Antigen I/II Participates in the Interactions ofFrontiers in cellular and infection microbiology · 2019Article
- Structural analysis and immunostimulatory potency of lipoteichoic acids isolated from threeThe Journal of biological chemistry · 2018Article
- Article
- Review
- Triggering Receptor Expressed on Myeloid Cells-1 Signaling: Protective and Pathogenic Roles on Streptococcal Toxic-Shock-Like Syndrome Caused byFrontiers in immunology · 2018Review
- Capsular Sialyltransferase Specificity Mediates Different Phenotypes inFrontiers in microbiology · 2018Article
- IgM cleavage by Streptococcus suis reduces IgM bound to the bacterial surface and is a novel complement evasion mechanism.Virulence · 2018Article
- Serotype-specific role of antigen I/II in the initial steps of the pathogenesis of the infection caused by Streptococcus suis.Veterinary research · 2017Article
- A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes.Scientific reports · 2017Article
- Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium.PloS one · 2017Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus suis is an important bacterial swine pathogen and a zoonotic agent. Recently, two surface proteins of S. suis, Fhb and Fhbp, have been described for their capacity to bind factor H-a soluble complement regulatory protein that protects host cells from complement-mediated damages. Results obtained in this study showed an important role of host factor H in the adhesion of S. suis to epithelial and endothelial cells. Both Fhb and Fhbp play, to a certain extent, a role in such increased factor H-dependent adhesion. The capsular polysaccharide (CPS) of S. suis, independently of the presence of its sialic acid moiety, was also shown to be involved in the recruitment of factor H. However, a triple mutant lacking Fhb, Fhbp and CPS was still able to recruit factor H resulting in the degradation of C3b in the presence of factor I. In the presence of complement factors, the double mutant lacking Fhb and Fhbp was similarly phagocytosed by human macrophages and killed by pig blood when compared to the wild-type strain. In conclusion, this study suggests that recruitment of factor H to the S. suis cell surface is multifactorial and redundant.
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