Korean J Parasitol.  2014 Dec;52(6):595-603. 10.3347/kjp.2014.52.6.595.

Trichomonas vaginalis Metalloproteinase Induces mTOR Cleavage of SiHa Cells

• Quan JH
• Choi IW
• Yang JB
• Zhou W
• Cha GH
• Zhou Y
• Ryu JS
• Lee YH

• KMID: 2069809
• DOI: http://doi.org/10.3347/kjp.2014.52.6.595

Abstract

Trichomonas vaginalis secretes a number of proteases which are suspected to be the cause of pathogenesis; however, little is understood how they manipulate host cells. The mammalian target of rapamycin (mTOR) regulates cell growth, cell proliferation, cell motility, cell survival, protein synthesis, and transcription. We detected various types of metalloproteinases including GP63 protein from T. vaginalis trophozoites, and T. vaginalis GP63 metalloproteinase was confirmed by sequencing and western blot. When SiHa cells were stimulated with live T. vaginalis, T. vaginalis excretory-secretory products (ESP) or T. vaginalis lysate, live T. vaginalis and T. vaginalis ESP induced the mTOR cleavage in both time- and parasite load-dependent manner, but T. vaginalis lysate did not. Pretreatment of T. vaginalis with a metalloproteinase inhibitor, 1,10-phenanthroline, completely disappeared the mTOR cleavage in SiHa cells. Collectively, T. vaginalis metallopeptidase induces host cell mTOR cleavage, which may be related to survival of the parasite.

Keyword

Trichomonas vaginalis; 1,10-phenanthroline; mTOR cleavage; SiHa cell; metalloproteinase

MeSH Terms

Blotting, Western
Cell Line, Tumor
Epithelial Cells/metabolism/parasitology
Humans
Metalloproteases/genetics/*metabolism
Proteolysis
Sequence Analysis, DNA
TOR Serine-Threonine Kinases/*metabolism
Trichomonas vaginalis/*enzymology/genetics
Metalloproteases
TOR Serine-Threonine Kinases