ArticleThe Journal of biological chemistry2011
Identification of a novel streptococcal adhesin P (SadP) protein recognizing galactosyl-α1-4-galactose-containing glycoconjugates: convergent evolution of bacterial pathogens to binding of the same host receptor.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.
- Identification ofVirulence · 2021Pooled it
- Innate immune response to Streptococcus suis infection: advances and future challenges.Veterinary research · 2026Review
- A novel SadP-scFv UCHT1 lectibody activates T cells and mediates lysis of Burkitt's lymphoma cells.RSC chemical biology · 2026Article
- Serovar-Dependent Gene Regulation and Antimicrobial Tolerance inAntibiotics (Basel, Switzerland) · 2025Article
- Amylase Binding to Oral Streptococci: A Key Interaction for Human Oral Microbial Ecology, Adaptation and Fitness.Biomolecules · 2025Review
- Human Gb3/CD77 synthase: a glycosyltransferase at the crossroads of immunohematology, toxicology, and cancer research.Cellular & molecular biology letters · 2024Review
- Structural Diversities of Lectins Binding to the Glycosphingolipid Gb3.Frontiers in molecular biosciences · 2021Review
- The interaction between flagellin and the glycosphingolipid Gb3 on host cells contributes toVirulence · 2020Article
- The binding mechanism of the virulence factorThe Journal of biological chemistry · 2020Article
- Comparative Virulence and Genomic Analysis ofFrontiers in microbiology · 2020Article
- Reinfection with Streptococcus suis analysed by whole genome sequencing.Zoonoses and public health · 2019Article
- Article
- Interaction of factor H-binding protein of Streptococcus suis with globotriaosylceramide promotes the development of meningitis.Virulence · 2017Article
- The Streptococcus suis factor H-binding protein: A key to unlocking the blood-brain barrier and access the central nervous system?Virulence · 2017Article
- The involvement of MsmK in pathogenesis of the Streptococcus suis serotype 2.MicrobiologyOpen · 2017Article
- Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium.PloS one · 2017Article
- Recruitment of Factor H to the Streptococcus suis Cell Surface is Multifactorial.Pathogens (Basel, Switzerland) · 2016Article
- A hypothetical model of host-pathogen interaction of Streptococcus suis in the gastro-intestinal tract.Gut microbes · 2016Review
- Host-pathogen Interaction at the Intestinal Mucosa Correlates With Zoonotic Potential of Streptococcus suis.The Journal of infectious diseases · 2015Article
- Blood Groups in Infection and Host Susceptibility.Clinical microbiology reviews · 2015Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial adhesion is often a prerequisite for infection, and host cell surface carbohydrates play a major role as adhesion receptors. Streptococci are a leading cause of infectious diseases. However, only few carbohydrate-specific streptococcal adhesins are known. Streptococcus suis is an important pig pathogen and a zoonotic agent causing meningitis in pigs and humans. In this study, we have identified an adhesin that mediates the binding of S. suis to galactosyl-α1-4-galactose (Galα1-4Gal)-containing host receptors. A functionally unknown S. suis cell wall protein (SSU0253), designated here as SadP (streptococcal adhesin P), was identified using a Galα1-4Gal-containing affinity matrix and LC-ESI mass spectrometry. Although the function of the protein was not previously known, it was recently identified as an immunogenic cell wall protein in a proteomic study. Insertional inactivation of the sadP gene abolished S. suis Galα1-4Gal-dependent binding. The adhesin gene sadP was cloned and expressed in Escherichia coli. Characterization of its binding specificity showed that SadP recognizes Galα1-4Gal-oligosaccharides and binds its natural glycolipid receptor, GbO(3) (CD77). The N terminus of SadP was shown to contain a Galα1-Gal-binding site and not to have apparent sequence similarity to other bacterial adhesins, including the E. coli P fimbrial adhesins, or to E. coli verotoxin or Pseudomonas aeruginosa lectin I also recognizing the same Galα1-4Gal disaccharide. The SadP and E. coli P adhesins represent a unique example of convergent evolution toward binding to the same host receptor structure.
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