Premium
Peptidase Activity of Dipeptidyl Aminopeptidase IV Produced by Porphyromonas gingivalis Is Important but Not Sufficient for Virulence
Author(s) -
Kumagai Yumi,
Yajima Ayako,
Konishi Kiyoshi
Publication year - 2003
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2003.tb03443.x
Subject(s) - porphyromonas gingivalis , virulence , biology , microbiology and biotechnology , aminopeptidase , mutant , virulence factor , dipeptidyl peptidase 4 , dipeptidyl peptidase , pathogen , gene , bacteria , genetics , enzyme , biochemistry , amino acid , leucine , type 2 diabetes , diabetes mellitus , endocrinology
Porphyromonas gingivalis is a pathogen associated with adult periodontitis, which is a chronic inflammatory disease characterized by breakdown of the periodontal tissue. Dipeptidyl aminopeptidase IV (DPPIV) produced by P. gingivalis has been considered to be a potential virulence factor based on the finding that the virulence was reduced by disruption of the gene ( dpp ) coding for DPPIV. In the present study, we constructed a shuttle vector that is mobilized from Escherichia coli to P. gingivalis and is maintained stably in both bacteria, and we showed that the virulence was restored by introducing the cloned wild‐type dpp gene into the null mutant of P. gingivalis using our vector system. To assess the implications of the peptidase activity in the virulence, mutant DPPIV with the catalytic Ser mutagenized to Ala (DPPSA) was produced. The P. gingivalis strain expressing DPPSA exhibited an intermediate virulence between the strain expressing wild‐type DPPIV and the strain harboring a vector. From these results, it is suggested that peptidase activity is very important but not sufficient for virulence.