Characterization of the zinc metalloprotease of Streptococcus suis serotype 2
Abstract Streptococcus suis is a swine pathogen and zoonotic agent responsible for meningitis and septic shock. Although several putative virulence factors have been described, the initial steps of the S. suis pathogenesis remain poorly understood. While controversial results have been reported for...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2018-10-01
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| Series: | Veterinary Research |
| Online Access: | http://link.springer.com/article/10.1186/s13567-018-0606-y |
| _version_ | 1828302543098216448 |
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| author | Audrey Dumesnil Jean-Philippe Auger David Roy Désirée Vötsch Maren Willenborg Peter Valentin-Weigand Pyong Woo Park Daniel Grenier Nahuel Fittipaldi Josée Harel Marcelo Gottschalk |
| author_facet | Audrey Dumesnil Jean-Philippe Auger David Roy Désirée Vötsch Maren Willenborg Peter Valentin-Weigand Pyong Woo Park Daniel Grenier Nahuel Fittipaldi Josée Harel Marcelo Gottschalk |
| author_sort | Audrey Dumesnil |
| collection | DOAJ |
| description | Abstract Streptococcus suis is a swine pathogen and zoonotic agent responsible for meningitis and septic shock. Although several putative virulence factors have been described, the initial steps of the S. suis pathogenesis remain poorly understood. While controversial results have been reported for a S. suis serotype 2 zinc metalloprotease (Zmp) regarding its IgA protease activity, recent phylogenetic analyses suggested that this protein is homologous to the ZmpC of Streptococcus pneumoniae, which is not an IgA protease. Based on the previously described functions of metalloproteases (including IgA protease and ZmpC), different experiments were carried out to study the activities of that of S. suis serotype 2. First, results showed that S. suis, as well as the recombinant Zmp, were unable to cleave human IgA1, confirming lack of IgA protease activity. Similarly, S. suis was unable to cleave P-selectin glycoprotein ligand-1 and to activate matrix metalloprotease 9, at least under the conditions tested. However, S. suis was able to partially cleave mucin 16 and syndecan-1 ectodomains. Experiments carried out with an isogenic Δzmp mutant showed that the Zmp protein was partially involved in such activities. The absence of a functional Zmp protein did not affect the ability of S. suis to adhere to porcine bronchial epithelial cells in vitro, or to colonize the upper respiratory tract of pigs in vivo. Taken together, our results show that S. suis serotype 2 Zmp is not a critical virulence factor and highlight the importance of independently confirming results on S. suis virulence by different teams. |
| first_indexed | 2024-04-13T13:38:06Z |
| format | Article |
| id | doaj.art-9e1981fbff244208b6be98f762a1314b |
| institution | Directory Open Access Journal |
| issn | 1297-9716 |
| language | English |
| last_indexed | 2024-04-13T13:38:06Z |
| publishDate | 2018-10-01 |
| publisher | BMC |
| record_format | Article |
| series | Veterinary Research |
| spelling | doaj.art-9e1981fbff244208b6be98f762a1314b2022-12-22T02:44:44ZengBMCVeterinary Research1297-97162018-10-0149111510.1186/s13567-018-0606-yCharacterization of the zinc metalloprotease of Streptococcus suis serotype 2Audrey Dumesnil0Jean-Philippe Auger1David Roy2Désirée Vötsch3Maren Willenborg4Peter Valentin-Weigand5Pyong Woo Park6Daniel Grenier7Nahuel Fittipaldi8Josée Harel9Marcelo Gottschalk10Swine and Poultry Infectious Diseases Research Center (CRIPA), Department of Pathology and Microbiology, Faculty of Veterinary Medicine, University of MontrealSwine and Poultry Infectious Diseases Research Center (CRIPA), Department of Pathology and Microbiology, Faculty of Veterinary Medicine, University of MontrealSwine and Poultry Infectious Diseases Research Center (CRIPA), Department of Pathology and Microbiology, Faculty of Veterinary Medicine, University of MontrealInstitute for Microbiology, University of Veterinary Medicine HannoverInstitute for Microbiology, University of Veterinary Medicine HannoverInstitute for Microbiology, University of Veterinary Medicine HannoverBoston Children’s Hospital, Harvard Medical SchoolSwine and Poultry Infectious Diseases Research Center (CRIPA), Department of Pathology and Microbiology, Faculty of Veterinary Medicine, University of MontrealPublic Health Ontario Laboratory Toronto, and Department of Laboratory Medicine and Pathobiology, University of TorontoSwine and Poultry Infectious Diseases Research Center (CRIPA), Department of Pathology and Microbiology, Faculty of Veterinary Medicine, University of MontrealSwine and Poultry Infectious Diseases Research Center (CRIPA), Department of Pathology and Microbiology, Faculty of Veterinary Medicine, University of MontrealAbstract Streptococcus suis is a swine pathogen and zoonotic agent responsible for meningitis and septic shock. Although several putative virulence factors have been described, the initial steps of the S. suis pathogenesis remain poorly understood. While controversial results have been reported for a S. suis serotype 2 zinc metalloprotease (Zmp) regarding its IgA protease activity, recent phylogenetic analyses suggested that this protein is homologous to the ZmpC of Streptococcus pneumoniae, which is not an IgA protease. Based on the previously described functions of metalloproteases (including IgA protease and ZmpC), different experiments were carried out to study the activities of that of S. suis serotype 2. First, results showed that S. suis, as well as the recombinant Zmp, were unable to cleave human IgA1, confirming lack of IgA protease activity. Similarly, S. suis was unable to cleave P-selectin glycoprotein ligand-1 and to activate matrix metalloprotease 9, at least under the conditions tested. However, S. suis was able to partially cleave mucin 16 and syndecan-1 ectodomains. Experiments carried out with an isogenic Δzmp mutant showed that the Zmp protein was partially involved in such activities. The absence of a functional Zmp protein did not affect the ability of S. suis to adhere to porcine bronchial epithelial cells in vitro, or to colonize the upper respiratory tract of pigs in vivo. Taken together, our results show that S. suis serotype 2 Zmp is not a critical virulence factor and highlight the importance of independently confirming results on S. suis virulence by different teams.http://link.springer.com/article/10.1186/s13567-018-0606-y |
| spellingShingle | Audrey Dumesnil Jean-Philippe Auger David Roy Désirée Vötsch Maren Willenborg Peter Valentin-Weigand Pyong Woo Park Daniel Grenier Nahuel Fittipaldi Josée Harel Marcelo Gottschalk Characterization of the zinc metalloprotease of Streptococcus suis serotype 2 Veterinary Research |
| title | Characterization of the zinc metalloprotease of Streptococcus suis serotype 2 |
| title_full | Characterization of the zinc metalloprotease of Streptococcus suis serotype 2 |
| title_fullStr | Characterization of the zinc metalloprotease of Streptococcus suis serotype 2 |
| title_full_unstemmed | Characterization of the zinc metalloprotease of Streptococcus suis serotype 2 |
| title_short | Characterization of the zinc metalloprotease of Streptococcus suis serotype 2 |
| title_sort | characterization of the zinc metalloprotease of streptococcus suis serotype 2 |
| url | http://link.springer.com/article/10.1186/s13567-018-0606-y |
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