ArticleFrontiers in cellular and infection microbiology2015
Proteomics identification of novel fibrinogen-binding proteins of Streptococcus suis contributing to antiphagocytosis.
Article in Frontiers in cellular and infection microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.
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Who cites it
35 citing papers in PubMed, 1 synthesis or guideline pooled it, 67 citations in OpenAlex.
- Identification ofVirulence · 2021Pooled it
- SSU_RS09155, a virulence-associated gene encoding a putative membrane of unknown function, that is essential for Streptococcus suis serotype 2 virulence.Veterinary research · 2026Article
- Identification and characterization of ugpE associated with the full virulence of Streptococcus suis.Veterinary research · 2025Article
- Genomic analysis and virulence of human Streptococcus suis serotype 14.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Article
- Egr-1 is a key regulator of the blood-brain barrier damage induced by meningitic Escherichia coli.Cell communication and signaling : CCS · 2024Article
- Fibrinogen induces inflammatory responses via the immune activating receptor LILRA2.Frontiers in immunology · 2024Article
- Cross-reactivity and sequence similarity between microbial transglutaminase and human tissue antigens.Scientific reports · 2023Article
- Dihydroartemisinin ameliorates innate inflammatory response induced byJournal of pharmaceutical analysis · 2023Article
- Blood-Brain Barrier Integrity Damage in Bacterial Meningitis: The Underlying Link, Mechanisms, and Therapeutic Targets.International journal of molecular sciences · 2023Review
- Virulence factors ofFrontiers in microbiology · 2022Review
- Article
- Neutrophils inMicroorganisms · 2021Review
- Review
- Quantitative proteomic analysis reveals that serine/threonine kinase is involved in Streptococcus suis virulence and adaption to stress conditions.Archives of microbiology · 2021Article
- Peptidomics Analysis of Virulent Peptides Involved inAnimals : an open access journal from MDPI · 2021Article
- Streptococcus suis serotype 2 enolase interaction with host brain microvascular endothelial cells and RPSA-induced apoptosis lead to loss of BBB integrity.Veterinary research · 2021Article
- Involvement of Various Enzymes in the Physiology and Pathogenesis ofVeterinary sciences · 2020Review
- Population structure, genetic diversity and pathotypes of Streptococcus suis isolated during the last 13 years from diseased pigs in Switzerland.Veterinary research · 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
- Processed Food Additive Microbial Transglutaminase and Its Cross-Linked Gliadin Complexes Are Potential Public Health Concerns in Celiac Disease.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus suis serotype 2 (SS2) induced sepsis and meningitis are often accompanied by bacteremia. However, the mechanism whereby it helps S. suis to evade PMN-mediated phagocytosis remain unclear. Because of the central roles of bacteria-human fibrinogen (hFg) interaction in innate immunity, here, a proteomics based Far-western blotting (PBFWB) was developed to identify the fibrinogen-binding surface proteins of S. suis (SsFBPs) on a large-scale. And then thirteen potential SsFBPs were identified by PBFWB and we selected seven potential surface proteins to further confirm their binding ability to hFg, of which the gene mutant strains of MRP displayed significantly decrease in binding to immobilized hFg. Additionally, the polyclonal antibodies against Enolase were found to significantly inhibit the binding of SS2 to hFg. Strikingly, MRP and Enolase were found to improve the antiphagocytic ability of SS2 to PMNs by interacting with hFg and enhance the survival of SS2 in human blood. Taken together, the PBFWB method provides useful clues to the bacteria-host interactions. These studies firstly disclose MRP and Enolase were involved in immune evasion of SS2 at least in part by binding to Fg, which make them potential targets for therapies for SS2 infection.
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