ArticleVirulence2015
The type II histidine triad protein HtpsC is a novel adhesion with the involvement of Streptococcus suis virulence.
Article in Virulence, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Ultrafast visual detection of Streptococcus suis via HtpsC-targeted LAMP-CRISPR-Cas12a coupled with lateral flow immunochromatography.FEBS open bio · 2026Article
- Innate immune response to Streptococcus suis infection: advances and future challenges.Veterinary research · 2026Review
- FtsZ contributes to cytoadhesion and interaction with host extracellular matrix components and plasminogen in Mycoplasma bovis.Veterinary research · 2025Article
- Recombinant Extracellular Factor Protein ofVaccines · 2025Article
- A multi-epitope subunit vaccine providing broad cross-protection against diverse serotypes of Streptococcus suis.NPJ vaccines · 2024Article
- Genomic and phenotypic analysis of invasive Streptococcus suis isolated in Spain reveals genetic diversification and associated virulence traits.Veterinary research · 2024Article
- A rapid colloidal gold immunochromatographic assay based on polyclonal antibodies against HtpsC protein for the detection ofFrontiers in microbiology · 2023Article
- Metal Homeostasis in Pathogenic Streptococci.Microorganisms · 2022Review
- Genome analysis provides insight into hyper-virulence of Streptococcus suis LSM178, a human strain with a novel sequence type 1005.Scientific reports · 2021Article
- The type II histidine triad protein HtpsC facilitates invasion of epithelial cells by highly virulent Streptococcus suis serotype 2.Journal of microbiology (Seoul, Korea) · 2021Article
- Collagen Binding Proteins of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- Inactivation of theVirulence · 2020Article
- Identification of novel pig and human immunoglobulin G-binding proteins and characterization of the binding regions of enolase from Streptococcus suis serotype 2.AMB Express · 2020Article
- Article
- The non-conserved region of MRP is involved in the virulence of Streptococcus suis serotype 2.Virulence · 2017Article
- Article
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Authors and funding
12 authors.
Funding
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Abstract
Streptococcal histidine triad proteins HTPs are widely distributed within the Streptococcus genus. Based on the phylogenetic relationship and domain composition, HTPs are classified into type I and type II subfamilies. Previous studies revealed that several pathogenic streptococci contain more than one htp gene. We found that the highly virulent strain of Streptococcus suis 2 (S. suis 2), 05ZYH33 encodes 3 HTPs, designated HtpsA (previously described as HtpS), HtpsB, and HtpsC. Among them, HtpsC is the only member that contains leucine-rich repeat (LRR) domains at the C-terminal. In this study, we demonstrated that the recombinant HtpsC could bind to 2 different components of human ECM complex laminin and fibronectin in vitro, suggesting that it is a novel adhesin of S. suis 2. Having constructed an htpsC mutant, we evaluated its role in the pathogenesis of the highly virulent S. suis 2 strain 05ZYH33. Our data showed that inactivation of htpsC significantly affected adherence of S. suis 2 to Hep-2 cells and shortened the survival of the bacteria in whole blood. Furthermore, deletion of htpsC significantly attenuated the virulence of S. suis 2 in mice. These results demonstrated that htpsC was involved in the pathogenesis of the highly virulent S. suis 2 strain 05ZYH33. In line with the observation, immunization with HtpsC significantly prolonged mice's survival after S. suis 05ZYH33 challenge, indicating its potential use in the vaccine development against S. suis.
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