Identification and characterization of four proteases produced by Streptococcus suis

被引:41
作者
Jobin, MC [1 ]
Grenier, D [1 ]
机构
[1] Univ Laval, Fac Med Dentaire, Grp Rech Ecol Buccale, Quebec City, PQ G1K 7P4, Canada
关键词
Streptococcus suis; protease; virulence factor;
D O I
10.1016/S0378-1097(03)00088-0
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Streptococcus suis is an important worldwide swine pathogen. In this study. we investigated the production of proteases by S. suis serotype 2. Proteases were identified and characterized using chromogenic and fluorogenic assays and zymography. An Arg-aminopeptidase with a molecular mass of 55 kDa was found to be both cell-associated and extracellular. Cell-associated chymotrypsin-like and caseinase activities, belonging to the scrine- and metalloprotease classes respectively, were also detected. Lastly, a dipeptidyl peptidase IV (DPP IV) with a molecular mass of 70 kDa was detected in both whole cells and culture supernatants of S. suis serotype 2. Arg-aminopeptidase, caseinase and DPP IV activities were detected in all strains of S. suis serotype 2 tested whereas the chymotrypsin-like activity was only detected in European virulent strains of serotype 2, The optimum pH for all four proteases was between 6 and 8, and the optimum temperature ranged from 25 to 42degreesC. This is the First report on the production of proteases by S. suis. Further investigations will determine the possible contribution of these proteases in the pathogenicity of S. suis serotype 2. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:113 / 119
页数:7
相关论文
共 27 条
[1]   Streptococcus suis serotype 2 mutants deficient in capsular expression [J].
Charland, N ;
Harel, J ;
Kobisch, M ;
Lacasse, S ;
Gottschalk, M .
MICROBIOLOGY-SGM, 1998, 144 :325-332
[2]   Characterization and protective activity of a monoclonal antibody against a capsular epitope shared by Streptococcus suis serotypes 1, 2 and 1/2 [J].
Charland, N ;
Jacques, M ;
Lacouture, S ;
Gottschalk, M .
MICROBIOLOGY-SGM, 1997, 143 :3607-3614
[3]   BIOSYNTHESIS AND METABOLISM OF ARGININE IN BACTERIA [J].
CUNIN, R ;
GLANSDORFF, N ;
PIERARD, A ;
STALON, V .
MICROBIOLOGICAL REVIEWS, 1986, 50 (03) :314-352
[4]   Contribution of fibronectin-binding protein to pathogenesis of Streptococcus suis serotype 2 [J].
de Greeff, A ;
Buys, H ;
Verhaar, R ;
Dijkstra, J ;
van Alphen, L ;
Smith, HE .
INFECTION AND IMMUNITY, 2002, 70 (03) :1319-1325
[5]   Streptococcus thermophilus cell wall-anchored proteinase:: Release, purification, and biochemical and genetic characterization [J].
Fernandez-Espla, MD ;
Garault, P ;
Monnet, V ;
Rul, F .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2000, 66 (11) :4772-+
[6]   Novel extracellular x-prolyl dipeptidyl-peptidase (DPP) from Streptococcus gordonii FSS2:: an emerging subfamily of viridans streptococcal x-prolyl DPPs [J].
Goldstein, JM ;
Banbula, A ;
Kordula, T ;
Mayo, JA ;
Travis, J .
INFECTION AND IMMUNITY, 2001, 69 (09) :5494-5501
[7]  
GOLSTEIN JM, 2002, INFECT IMMUN, V70, P836
[8]   The pathogenesis of the meningitis caused by Streptococcus suis:: the unresolved questions [J].
Gottschalk, M ;
Segura, M .
VETERINARY MICROBIOLOGY, 2000, 76 (03) :259-272
[9]   IDENTIFICATION, PURIFICATION, AND CHARACTERIZATION OF A THIOL-ACTIVATED HEMOLYSIN (SUILYSIN) OF STREPTOCOCCUS-SUIS [J].
JACOBS, AAC ;
LOEFFEN, PLW ;
VANDENBERG, AJG ;
STORM, PK .
INFECTION AND IMMUNITY, 1994, 62 (05) :1742-1748
[10]  
Kähne T, 1999, INT J MOL MED, V4, P3