ArticleThe Journal of biological chemistry2015
Functional and Structural Characterization of the Antiphagocytic Properties of a Novel Transglutaminase from Streptococcus suis.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Innate immune response to Streptococcus suis infection: advances and future challenges.Veterinary research · 2026Review
- Antimicrobial and antivirulence function of cinnamaldehyde againstMicrobiology spectrum · 2025Article
- Identification of novel toxins associated with the extracellular contractile injection system using machine learning.Molecular systems biology · 2024Article
- Investigation of choline-binding protein of CbpD in the pathogenesis ofFrontiers in veterinary science · 2024Article
- Cross-reactivity and sequence similarity between microbial transglutaminase and human tissue antigens.Scientific reports · 2023Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Microbiological transglutaminase: Biotechnological application in the food industry.Open life sciences · 2023Review
- Gluten-free diet exposure prohibits pathobiont expansion and gluten sensitive enteropathy in B cell deficient JH-/- mice.PloS one · 2022Article
- Review
- Screening for phagocytosis resistance-related genes via a transposon mutant library ofVirulence · 2020Article
- Antibodies against neo-epitope of microbial and human transglutaminase complexes as biomarkers of childhood celiac disease.Clinical and experimental immunology · 2020Article
- Probiotics: If It Does Not Help It Does Not Do Any Harm. Really?Microorganisms · 2019Review
- Microbial Transglutaminase Is Immunogenic and Potentially Pathogenic in Pediatric Celiac Disease.Frontiers in pediatrics · 2018Review
- Potential Effects of Horizontal Gene Exchange in the Human Gut.Frontiers in immunology · 2017Article
- Microbial inhibitors of cysteine proteases.Medical microbiology and immunology · 2016Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus suis serotype 2 (Ss2) is an important swine and human zoonotic pathogen. In the present study, we identified a novel secreted immunogenic protein, SsTGase, containing a highly conserved eukaryotic-like transglutaminase (TGase) domain at the N terminus. We found that inactivation of SsTGase significantly reduced the virulence of Ss2 in a pig infection model and impaired its antiphagocytosis in human blood. We further solved the crystal structure of the N-terminal portion of the protein in homodimer form at 2.1 Å. Structure-based mutagenesis and biochemical studies suggested that disruption of the homodimer directly resulted in the loss of its TGase activity and antiphagocytic ability. Characterization of SsTGase as a novel virulence factor of Ss2 by acting as a TGase would be beneficial for developing new therapeutic agents against Ss2 infections.
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