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Journal of Bacteriology, January 2005, p. 795-799, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.795-799.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Cloning, Purification, and Enzymatic Properties of Dipeptidyl Peptidase IV from the Swine Pathogen Streptococcus suis

Marie-Claude Jobin,1 Gabriela Martinez,2 Julie Motard,1 Marcelo Gottschalk,2,3 and Daniel Grenier1,3*

Groupe de Recherche en Écologie Buccale, Faculté de Médecine Dentaire, Université Laval, Quebec City,1 Groupe de Recherche sur les Maladies Infectieuses du Porc, Faculté de Médecine Vétérinaire, Université de Montréal,2 Canadian Research Network on Bacterial Pathogens of Swine, Natural Sciences and Engineering Research Council of Canada, Saint-Hyacinthe, Quebec, Canada3

Received 5 July 2004/ Accepted 15 October 2004

In this study, the dipeptidyl peptidase IV (DPP IV) of the swine pathogen Streptococcus suis was cloned, overexpressed in Escherichia coli, and characterized. The coding region comprises 2,268 nucleotides containing an open reading frame that codes for a 755-amino-acid protein with a calculated molecular mass of 85 kDa. The amino acid sequence contained the sequence Gly-X-Ser-X-X-Gly, which is a consensus motif flanking the active-site serine shared by serine proteases. The recombinant DPP IV showed a high affinity for the synthetic peptide glycine-proline-p-nitroanilide and was strongly inhibited by Hg2+ and diprotin A.

* Corresponding author. Mailing address: Groupe de Recherche en Écologie Buccale, Faculté de Médecine Dentaire, Université Laval, Quebec City, Quebec, Canada G1K 7P4. Phone: (418) 656-7341. Fax: (418) 656-2861. E-mail: Daniel.Grenier{at}greb.ulaval.ca.

Journal of Bacteriology, January 2005, p. 795-799, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.795-799.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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