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PHD : Parasites, Hosts and Diseases

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Original Article

Trichomonas vaginalis Metalloproteinase Induces mTOR Cleavage of SiHa Cells

The Korean Journal of Parasitology 2014;52(6):595-603.
Published online: December 23, 2014

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Corresponding author (yhalee@cnu.ac.kr)

Juan-Hua Quan, In-Wook Choi, and Jung-Bo Yang contributed equally to this work.

• Received: April 8, 2014   • Revised: September 4, 2014   • Accepted: September 29, 2014

© 2014, Korean Society for Parasitology and Tropical Medicine

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Trichomonas vaginalis Metalloproteinase Induces mTOR Cleavage of SiHa Cells
Korean J Parasitol. 2014;52(6):595-603.   Published online December 23, 2014
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Trichomonas vaginalis Metalloproteinase Induces mTOR Cleavage of SiHa Cells
Korean J Parasitol. 2014;52(6):595-603.   Published online December 23, 2014
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Trichomonas vaginalis Metalloproteinase Induces mTOR Cleavage of SiHa Cells
Image Image Image Image Image Image
Fig. 1 T. vaginalis T016 isolate expressing several metalloproteinases. GP63 (501 bp), MP50 (304 bp), TVAG_243780.2 (598 bp), TVAG_477180 (800 bp), TVAG_075740 (400 bp), and TVAG_392410 (249 bp) metalloproteinase mRNA expression levels were detected by RT-PCR.
Fig. 2 The GP63 nucleotide sequences of recombinant plasmid pET32a-GP63 were compared with GenBank sequence (accession no. GU356538.1). Base homologies were indicated with blue, and base changes were shown in white. The total length of T. vaginalis T016 isolate GP63 region is 1,893 bp.
Fig. 3 Expression and identification of recombinant proteins. (A) Proteins were submitted to SDS-PAGE and revealed by Coomassie blue staining. M, protein molecular size marker; lane 1, pET32a-GP63 transfomed E. coli; lane 2, IPTG-induced pET32a-GP63 transfomed E. coli. (B) Western blot analysis of E. coli lysate with anti-His primary antibody. Lane 1, pET32a-GP63 transfomed E. coli lysate; lane 2, IPTG-induced pET32a-GP63 transfomed E. coli lysate.
Fig. 4 Live T. vaginalis and T. vaginalis ESP induced cleavage of host cell mTOR. After SiHa cells were incubated with live T. vaginalis at a multiplicity of infection (MOI) 2, T. vaginalis ESP (transwell) or T. vaginalis lysate (100 µg/ml) for 16 hr, protein levels of mTOR, AKT, and p70S6K were shown by western blot. Anti-α-tubulin antibodies were employed to confirm equal loading of the cell extracts. A representative result of 3 independent replicates is shown.
Fig. 5 T. vaginalis-induced cleavage of host cell mTOR is time- and parasite load-dependent manner. After SiHa cells were incubated with (A) T. vaginalis at MOI 2 for the indicated time points or (B) SiHa cells were infected with T. vaginalis at MOI 0.5, 1, and 2 for 2 hr, cells were collected, and levels of mTOR was measured. Anti-α-tubulin antibodies were employed to confirm equal loading of the cell extracts. A representative result of 3 independent replicates is shown.
Fig. 6 Cleavage of host cell mTOR induced by T. vaginalis was inhibited with metallopeptidase inhibitor, 1,10-phenanthroline (1,10-PT). T. vaginalis (MOI 2) were treated for 30 min with 1,10-PT (5 mM), and the control group T. vaginalis were mock-treated in PBS, and then T. vaginalis were washed with PBS and infected with SiHa cells. After 16 hr later, (A-C) cells were visualized under phage-contrast microscope, and (D) western blot was performed in order to detect mTOR. Anti-α-tubulin antibodies were employed to confirm equal loading of the cell extracts. A representative result of 3 independent replicates is shown. *, SiHa cell; #, trophozoite of T. vaginalis.
Trichomonas vaginalis Metalloproteinase Induces mTOR Cleavage of SiHa Cells
Gene Primer sequence GenBank accession no. PCR product size (bp) GP63 (F) ACGCTGTCCTTGCAATTCTT GU356538.1 501 (R) TTGCGTTTTCTTTTGTGCAT MP50 (F) TCTCGACTGCGGATTCTTCT JF263458.1 304 (R) TCCGACGTGATGAGTCAAAC TVAG_243780.2 (F) TGCAACAAATAGGGCAGACA KF269491.1 598 (R) AGCCCTCTCAATGTCGTTTG TVAG_477180 (F) TGTCCTCAAACCATGGAACA XM_001583725.1 800 (R) ATTTGTCGGCAACAACATCA TVAG_075740 (F) ATTCCCTGAGTGGGCTTTTT XM_001583763.1 400 (R) TGGATGCGTACGAGCAACTA TVAG_392410 (F) GTCGCATCAGAGCGTATTGA XM_001327312.1 249 (R) CCATGCGTGAGCATTATCTG TVAG_077490 (F) AGCCAACGAAACAGACTTCC XM_001325199.1 201 (R) ATGATGTGATGGTGCTTGGA TVAG_371040 (F) CGCCGAGACAAACAGAGAAT XM_001300222.1 899 (R) GATCAGCACCATGAATCCAA
Table 1. Primers used for detection of various kinds of metalloproteinases from Trichomonas vaginalis