ArticleBMC microbiology2010
The cell envelope subtilisin-like proteinase is a virulence determinant for Streptococcus suis.
Article in BMC microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 60 citations in OpenAlex.
- Analysis of Antimicrobial Resistance and Virulence Factors in Multidrug-ResistantMicroorganisms · 2025Article
- Functional study of Bergeyella cardium KP-43 subfamily peptidases as putative T9SS cargo.Communications biology · 2025Article
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- A multi-epitope subunit vaccine providing broad cross-protection against diverse serotypes of Streptococcus suis.NPJ vaccines · 2024Article
- Novel virulence factor Cba induces antibody-dependent enhancement (ADE) ofFrontiers in cellular and infection microbiology · 2023Article
- Genome-Wide Analysis and Characterization of the Riemerella anatipestifer Putative T9SS Secretory Proteins with a Conserved C-Terminal Domain.Journal of bacteriology · 2022Article
- Riemerella anatipestifer T9SS Effector SspA Functions in Bacterial Virulence and Defending Natural Host Immunity.Applied and environmental microbiology · 2022Article
- Screening for Virulence-Related Genes via a Transposon Mutant Library ofMicroorganisms · 2022Article
- The Role of Streptococcal Cell-Envelope Proteases in Bacterial Evasion of the Innate Immune System.Journal of innate immunity · 2022Review
- Trans-2-hexenal downregulates several pathogenicity genes of Pseudogymnoascus destructans, the causative agent of white-nose syndrome in bats.Journal of industrial microbiology & biotechnology · 2021Article
- Role of the Sortase A in the Release of Cell-Wall Proteinase PrtS in the Growth Medium ofMicroorganisms · 2021Article
- Gene Analysis, Cloning, and Heterologous Expression of Protease from a MicromyceteMicroorganisms · 2021Article
- Immunogenicity and protective efficacy of a Streptococcus suis vaccine composed of six conserved immunogens.Veterinary research · 2021Article
- Pneumococcal Extracellular Serine Proteases: Molecular Analysis and Impact on Colonization and Disease.Frontiers in cellular and infection microbiology · 2021Review
- Application of phage display technology for the production of antibodies against Streptococcus suis serotype 2.PloS one · 2021Article
- Involvement of Various Enzymes in the Physiology and Pathogenesis ofVeterinary sciences · 2020Review
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- Article
- Mac Protein is not an Essential Virulence Factor for the Virulent Reference Strain Streptococcus suis P1/7.Current microbiology · 2017Article
- Subtilisin-like protease-1 secreted through type IV secretion system contributes to high virulence of Streptococcus suis 2.Scientific reports · 2016Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundStreptococcus suis is a major swine pathogen and zoonotic agent that mainly causes septicemia, meningitis, and endocarditis. It has recently been suggested that proteinases produced by S. suis (serotype 2) are potential virulence determinants. In the present study, we screened a S. suis mutant library created by the insertion of Tn917 transposon in order to isolate a mutant deficient in a cell surface proteinase. We characterized the gene and assessed the proteinase for its potential as a virulence factor.
resultsTwo mutants (G6G and M3G) possessing a single Tn917 insertion were isolated. The affected gene coded for a protein (SSU0757) that shared a high degree of identity with Streptococccus thermophilus PrtS (95.9%) and, to a lesser extent, with Streptococcus agalactiae CspA (49.5%), which are cell surface serine proteinases. The SSU0757 protein had a calculated molecular mass of 169.6 kDa and contained the catalytic triad characteristic of subtilisin family proteinases: motif I (Asp200), motif II (His239), and motif III (Ser568). SSU0757 also had the Gram-positive cell wall anchoring motif (Leu-Pro-X-Thr-Gly) at the carboxy-terminus, which was followed by a hydrophobic domain. All the S. suis isolates tested, which belonged to different serotypes, possessed the gene encoding the SSU0757 protein. The two mutants devoid of subtilisin-like proteinase activity had longer generation times and were more susceptible to killing by whole blood than the wild-type parent strain P1/7. The virulence of the G6G and M3G mutants was compared to the wild-type strain in the CD1 mouse model. Significant differences in mortality rates were noted between the P1/7 group and the M3G and G6G groups (p < 0.001).
conclusionIn summary, we identified a gene coding for a cell surface subtilisin-like serine proteinase that is widely distributed in S. suis. Evidences were brought for the involvement of this proteinase in S. suis virulence.
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