{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T03:07:23Z","timestamp":1789873643178,"version":"4.0.1"},"reference-count":50,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2004,7,1]],"date-time":"2004-07-01T00:00:00Z","timestamp":1088640000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2004,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Tritrichomonas foetus<\/jats:italic>\n                    is a serious veterinary pathogen, causing bovine trichomoniasis, a sexually transmitted disease leading to infertility and abortion.\n                    <jats:italic>T. foetus<\/jats:italic>\n                    infects the mucosal surfaces of the reproductive tract. Infection with\n                    <jats:italic>T. foetus<\/jats:italic>\n                    leads to apoptotic cell death of bovine vaginal epithelial cells (BVECs) in culture. An affinity-purified cysteine protease (CP) fraction yielding on sodium dodecyl sulfate-polyacrylamide gel electrophoresis a single band with an apparent molecular mass of 30 kDa (CP30) also induces BVEC apoptosis. Treatment of CP30 with the protease inhibitors TLCK (\n                    <jats:italic>N<\/jats:italic>\n                    \u03b1-\n                    <jats:italic>p<\/jats:italic>\n                    -tosyl-\n                    <jats:sc>l<\/jats:sc>\n                    -lysine chloromethyl ketone) and E-64 [\n                    <jats:sc>l<\/jats:sc>\n                    -\n                    <jats:italic>trans<\/jats:italic>\n                    -epoxysuccinyl-leucylamide-(4-guanido)-butane] greatly reduces induction of BVEC apoptosis. Matrix-assisted laser desorption ionization-time-of-flight MALDI-TOF mass spectrometry analysis of CP30 reveals a single peak with a molecular mass of 23.7 kDa. Mass spectral peptide sequence analysis of proteolytically digested CP30 reveals homologies to a previously reported cDNA clone, CP8 (D. J. Mallinson, J. Livingstone, K. M. Appleton, S. J. Lees, G. H. Coombs, and M. J. North, Microbiology\n                    <jats:bold>141:<\/jats:bold>\n                    3077-3085, 1995). Induction of apoptosis is highly species specific, since the related human parasite\n                    <jats:italic>Trichomonas vaginalis<\/jats:italic>\n                    and associated purified CPs did not induce BVEC death. Fluorescence microscopy along with the Cell Death Detection ELISA\n                    <jats:sup>PLUS<\/jats:sup>\n                    assay and flow cytometry analyses were used to detect apoptotic nuclear condensation, DNA fragmentation, and changes in plasma membrane asymmetry in host cells undergoing apoptosis in response to\n                    <jats:italic>T. foetus<\/jats:italic>\n                    infection or incubation with CP30. Additionally, the activation of caspase-3 and inhibition of cell death by caspase inhibitors indicates that caspases are involved in BVEC apoptosis. These results imply that apoptosis is involved in the pathogenesis of\n                    <jats:italic>T. foetus<\/jats:italic>\n                    infection in vivo, which may have important implications for therapeutic interference with host cell death that could alter the course of the pathology in vivo.\n                  <\/jats:p>","DOI":"10.1128\/iai.72.7.4151-4158.2004","type":"journal-article","created":{"date-parts":[[2004,6,22]],"date-time":"2004-06-22T18:43:13Z","timestamp":1087929793000},"page":"4151-4158","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":52,"title":["<i>Tritrichomonas foetus<\/i>\n                    Induces Apoptotic Cell Death in Bovine Vaginal Epithelial Cells"],"prefix":"10.1128","volume":"72","author":[{"given":"B. N.","family":"Singh","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. J.","family":"Lucas","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G. R.","family":"Hayes","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ish","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D. H.","family":"Beach","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, SUNY Upstate Medical University, Syracuse, New York 13210"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcel","family":"Frajblat","sequence":"additional","affiliation":[{"name":"Department of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. O.","family":"Gilbert","sequence":"additional","affiliation":[{"name":"Department of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"U.","family":"Sommer","sequence":"additional","affiliation":[{"name":"Boston University School of Medicine Mass Spectrometry Resource, Boston, Massachusetts 02118"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. 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