Korean J Parasitol.  1993 Jun;31(2):117-127. 10.3347/kjp.1993.31.2.117.

Proteinase activity in the isolates of Trichomonas vaginalis according to their pathogenicity

• Shim YK
• Park KH
• Chung PR
• Im KI

• KMID: 1715480
• DOI: http://doi.org/10.3347/kjp.1993.31.2.117

Abstract

Ten axenic isolates of Trichomonas vaginalis were subcutaneously injected to the BALB/c mice in order to assess their pathogenicity by means of so-called "mouse assay" method. All the isolates revealed neutral and acid proteinase activities both in their lysates and in culture media, but the specific activities of both proteinases in the severely pathogenic group were significantly higher than the mildly pathogenic group (p < 0.05). In the SDS-PAGE system in which the electrophoretic gels contained 0.4% gelatin as the substrate, five different banding patterns of trichomonal proteinases were detected, and the patterns were closely related with the pathogenicity of the isolates of T. vaginalis. All five bands might be regarded as cysteine proteinases group in the inhibitor assays. The cytotoxicity of the lysates of T. vaginalis to the target Chinese hamster ovarian (CHO) cell line was also significantly different according to the pathogenicity of the isolates, and generally lower in the lysates treated with cysteine proteinase inhibitors than in the control lysates. In summarizing the results, it might be considered that the proteinases of T. vaginalis showing five electrophoretic banding patterns are closely related with the pathogenicity and cytotoxicity of the isolates of T. vaginalis.

MeSH Terms

Adult-
CHO-Cells
Electrophoresis,-Polyacrylamide-Gel
English-Abstract
Hamsters-
Mice-
Mice,-Inbred-BALB-C
Middle-Age
*Peptide-Peptidohydrolases-metabolism
*Trichomonas-vaginalis-enzymology
*Trichomonas-vaginalis-pathogenicity
Peptide-Peptidohydrolases