The cell envelope subtilisin-like proteinase is a virulence determinant for Streptococcus suis
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- 作者：Laetitia Bonifait (1)
Maria de la Cruz Dominguez-Punaro (2)
Katy Vaillancourt (1)
Christian Bart (1)
Josh Slater (3)
Michel Frenette (1)
Marcelo Gottschalk (2)
Daniel Grenier (1) - 刊名：BMC Microbiology
- 出版年：2010
- 出版时间：December 2010
- 年：2010
- 卷：10
- 期：1
- 全文大小：708KB
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Maria de la Cruz Dominguez-Punaro (2)
Katy Vaillancourt (1)
Christian Bart (1)
Josh Slater (3)
Michel Frenette (1)
Marcelo Gottschalk (2)
Daniel Grenier (1)
1. Groupe de Recherche en 脡cologie Buccale, Facult茅 de M茅decine Dentaire, Universit茅 Laval, Quebec City, Quebec, Canada
2. Groupe de Recherche sur les Maladies Infectieuses du Porc, Facult茅 de M茅decine V茅t茅rinaire, Universit茅 de Montr茅al, Saint-Hyacinthe, Quebec, Canada
3. The Royal Veterinary College, Hatfield, UK - ISSN：1471-2180
文摘
Background Streptococcus 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. Results Two 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). Conclusion In 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.