The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65

Kucknoor, Ashwini S.; Mundodi, Vasanthakrishna; Alderete, John F.

doi:10.1111/j.1462-5822.2007.00979.x

Cited by 56 publications

(63 citation statements)

References 59 publications

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“…We showed earlier that brief contact of trichomonads with VECs produced dramatic changes in parasite morphology (9) in addition to synthesis of adhesins and other trichomonad proteins (26), suggesting host-specific signaling of parasites. More recently, we showed that parasite contact with VECs (24) and the released proteins of T. vaginalis (27), the majority of which were metabolic enzymes, including tv-ENO1, induced expression of numerous VEC genes. We now confirm that T. vaginalis tv-ENO1 is released and at the same time is present on the parasite surface.…”

Section: Discussionmentioning

confidence: 99%

“…It is known that secretions of patients contain numerous trichomonad proteins, including high-molecular-weight immunogenic proteins (3) and cysteine proteinases (5). Further, it is known that numerous proteins are readily released during growth, and multiplication without lysis of organisms has been established (2,27).…”

Section: Discussionmentioning

confidence: 99%

“…Parasites were monitored during growth and incubation periods to assure the absence of cell lysis (2). Supernatant was clarified by gentle centrifugation at 500 ϫ g at 4°C as described before (2,27). Despite the absence of lysis, the resulting supernatant was filtered through a 0.22-m-pore-size filter to remove insoluble debris.…”

Section: Methodsmentioning

confidence: 99%

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Immunogenic and Plasminogen-Binding Surface-Associated α-Enolase of Trichomonas vaginalis

2008

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Trichomonas vaginalis is a protist that causes the most common human sexually transmitted infection. A T. vaginalis cDNA expression library was screened with pooled sera from patients with trichomoniasis. A highly reactive cDNA clone of 1,428 bp encoded a trichomonad protein of 472 amino acids with sequence identity to ␣-enolase (tv-eno1). The sequence alignment confirmed the highly conserved nature of the enzyme with 65% to 84% identity among organisms. The expression of tv-eno1 was up-regulated by contact of parasites with vaginal epithelial cells, and this is the first report demonstrating up-regulation by cytoadherence of a plasminogenbinding ␣-enolase in T. vaginalis. Immunofluorescence with monoclonal antibody of nonpermeabilized trichomonads showed tv-ENO1 on the surface. The recombinant tv-ENO1 was expressed in Escherichia coli as a glutathione S-transferase (GST)::tv-ENO1 fusion protein, which was cleaved using thrombin to obtain affinity-purified recombinant tv-ENO1 protein (tv-rENO1) detectable in immunoblots by sera of patients. Immobilized tv-rENO1 bound human plasminogen in a dose-dependent manner, and plasminogen binding by tv-rENO1 was confirmed in a ligand blot assay. The plasminogen-specific inhibitor -aminocaproic acid blocked the tv-rENO1-plasminogen association, indicating that lysines play a role in binding to tv-rENO1. Further, both parasites and tv-rENO1 activate plasminogen to plasmin that is mediated by tissue plasminogen activator. These data indicate that as with other bacterial pathogens, tv-ENO1 is an anchorless, surfaceassociated glycolytic enzyme of T. vaginalis.Trichomonas vaginalis is responsible for the number one, nonviral sexually transmitted disease worldwide (56). There are 250 million new cases of trichomoniasis worldwide and ϳ9 million cases in the United States (15,55,57). Trichomoniasis is known to increase the portal of entry and exit for human immunodeficiency virus (51). A recent study showed serological evidence linking trichomoniasis with prostate cancer (52). Given the significant human morbidity caused by T. vaginalis, there is a need for identifying virulence factors and elucidating the mechanisms of disease pathogenesis.A prerequisite for T. vaginalis infection is its ability to colonize the vaginal epithelium. Surface-associated adhesin proteins were shown to be involved in parasite adherence to vaginal epithelial cells (VECs) (4,19,20). There is a direct relationship between the amount of surface adhesin that binds to host cells in a ligand-receptor type interaction (8,20) and the level of cytoadherence (8,20). Contact with VECs produces a dramatic change in morphology accompanied by synthesis of adhesins (9, 26). A recent study using antisense RNA reaffirmed the importance of AP65 and AP33 in parasite associations with VECs (37, 38). In addition, heterologous expression of AP65 and AP33 on the Tritrichomonas foetus surface provided evidence that both are bona fide adhesins of T. vaginalis (25,38). Interestingly, these adhesins show sequence identity to metab...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Immunogenic and Plasminogen-Binding Surface-Associated α-Enolase of Trichomonas vaginalis

2008

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“…Differentially expressed protein spots in the amoeboid stage compared with the trophozoite stage are marked by arrows and protein spot numbers. tively, it is conceivable that, if secreted by the parasite, as has been found for numerous other proteins (43), this insulin-like GF may influence the host cell. Of interest in the future will be whether host hormones signal for trichomonal growth and multiplication.…”

Section: Fig 3 2-de Maps Of Trophozoites and Fn-bound Amoeboid Cells mentioning

confidence: 99%

Comparative Transcriptomic and Proteomic Analyses of Trichomonas vaginalis following Adherence to Fibronectin

Huang

et al. 2012

Infect Immun

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FN-binding protein), and stress-related proteins were upregulated in the FN-adherent cells. Stress-related genes and proteins were highly expressed in both the transcriptome and proteome of FN-bound organisms, implying that these genes and proteins may play critical roles in the response to adherence. This is the first report of a comparative proteomic and transcriptomic analysis after the binding of T. vaginalis to FN. This approach may lead to the discovery of novel virulence genes and affirm the role of genes involved in disease pathogenesis. This knowledge will permit a greater understanding of the complex host-parasite interplay.

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“…Although in the literature it is routinely reported that men infected by their partners resolve their infections, there is neither experimental evidence nor clinical studies proving this. Reports have shown the expression of numerous virulence factors that permit this ancient protist to survive in the changing host environment of the female urogenital region (3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18). Iron is an important modulator of upregulation and downregulation of the expression of virulence genes (8,(19)(20)(21)(22)(23)(24)(25).…”

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confidence: 99%

Epitopes of the Highly Immunogenic Trichomonas vaginalis α-Actinin Are Serodiagnostic Targets for Both Women and Men

2013

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There is a need for a point-of-care serodiagnostic test for women and men for sexually transmitted infections (STIs) caused by Trichomonas vaginalis. Sera from women with this STI and sera from men that were analyzed in studies showing a relationship between serostatus and prostate cancer are highly seropositive in response to trichomonad ␣-actinin and its truncated protein (ACT-P2) (positive control sera). Epitope mapping experiments showed that positive control sera from women had antibodies to 13 distinct epitopes, 5 of which were detected by positive control sera from men. Sera from women and men that were unreactive with ␣-actinin (negative control sera) failed to detect any of the epitopes or other ␣-actinin amino acid sequences. The T. vaginalis ␣-actinin amino acid sequence and the sequences of the epitopes showed little or no identity with those of other proteins of microbial pathogens or the human ␣-actinin 1 (HuACTN1) homolog. Immunoassays such as dot blot, immunoblot, and enzyme-linked immunosorbent assays were used. Positive control sera did not detect HuACTN1 in immunoassays, and the range of levels of identity of ␣-actinin epitopes with HuACTN1 was 0% to 50%. Comparison of the T. vaginalis ␣-actinin epitopes with proteins in data banks, such as Tritrichomonas suis, Candida albicans, and Saccharomyces cerevisiae proteins, gave a range of identity levels of 0% to 22%. Specific 15-mer peptide epitopes of ␣-actinin with low to no identity with other proteins were synthesized and were reactive with positive control sera only. These findings identify epitopes of ␣-actinin as candidate serodiagnostic targets and suggest strongly that a highly seropositive reaction to ␣-actinin suggests exposure to T. vaginalis.T richomonas vaginalis is the most common nonviral causative agent for sexually transmitted infections (STIs). The adverse consequences for the health of women have been well documented (1, 2). Although in the literature it is routinely reported that men infected by their partners resolve their infections, there is neither experimental evidence nor clinical studies proving this. Reports have shown the expression of numerous virulence factors that permit this ancient protist to survive in the changing host environment of the female urogenital region (3-18). Iron is an important modulator of upregulation and downregulation of the expression of virulence genes (8,(19)(20)(21)(22)(23)(24)(25). Key steps for host colonization result from overcoming the urogenital mucous layer (18) in preparation for specific cytoadherence to vaginal epithelial cells (7,9,11,22,24). The intimacy of the host-parasite relationship during colonization and infection is exceedingly complex, as evidenced by the large number of proteinases (4,11,15,26) and the secretion by trichomonads of large amounts of putrescine for spermine uptake and back-conversion to spermidine (13,26). This coating of T. vaginalis by polyamines and host macromolecules affects levels of cytoadherence and cytotoxicity (3, 13).More recently, epidemiologic...

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The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65

Cited by 56 publications

References 59 publications

Immunogenic and Plasminogen-Binding Surface-Associated α-Enolase of Trichomonas vaginalis

Immunogenic and Plasminogen-Binding Surface-Associated α-Enolase of Trichomonas vaginalis

Comparative Transcriptomic and Proteomic Analyses of Trichomonas vaginalis following Adherence to Fibronectin

Epitopes of the Highly Immunogenic Trichomonas vaginalis α-Actinin Are Serodiagnostic Targets for Both Women and Men

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