Parasites, Hosts and Diseases

  • 제49권1호
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  • Pages.79-83
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  • 2011
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  • 2982-5164(pISSN)
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  • 1738-0006(eISSN)
대한기생충학·열대의학회 (The Korea Society for Parasitology and Tropical Medicine)
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Identification of Antigenic Proteins in Trichomonas vaginalis

  • Lee, Hye-Yeon (Department of Environmental Medical Biology and Institute of Tropical Medicine, Post Brain Korea 21 Program, Yonsei University College of Medicine) ;
  • Hyung, Su-Jin (Department of Environmental Medical Biology and Institute of Tropical Medicine, Post Brain Korea 21 Program, Yonsei University College of Medicine) ;
  • Lee, Jong-Woong (Department of Environmental Medical Biology and Institute of Tropical Medicine, Post Brain Korea 21 Program, Yonsei University College of Medicine) ;
  • Kim, Ju-Ri (Department of Environmental Medical Biology and Institute of Tropical Medicine, Post Brain Korea 21 Program, Yonsei University College of Medicine) ;
  • Shin, Myeong-Heon (Department of Environmental Medical Biology and Institute of Tropical Medicine, Post Brain Korea 21 Program, Yonsei University College of Medicine) ;
  • Ryu, Jae-Sook (Department of Environmental Medical Biology, Hanyang University College of Medicine) ;
  • Park, Soon-Jung (Department of Environmental Medical Biology and Institute of Tropical Medicine, Post Brain Korea 21 Program, Yonsei University College of Medicine)
  • 투고 : 2010.11.22
  • 심사 : 2011.01.29
  • 발행 : 2011.03.15
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초록

Trichomoniasis is a sexually transmitted disease due to infection with Trichomonas vaginalis, and it can cause serious consequences for women's health. To study the virulence factors of this pathogen, T. vaginalis surface proteins were investigated using polyclonal antibodies specific to the membrane fractions of T. vaginalis. The T. vaginalis expression library was constructed by cloning the cDNA derived from mRNA of T. vaginalis into a phage ${\lambda}$ Uni-ZAP XR vector, and then used for immunoscreening with the anti-membrane proteins of T. vaginalis antibodies. The immunoreactive proteins identified included adhesion protein AP65-1, ${\alpha$-actinin, kinesin-associated protein, teneurin, and 2 independent hypothetical proteins. Immunofluorescence assays showed that AP65-1, one of the identified immunogenic clones, is prevalent in the whole body of T. vaginalis. This study led us to identify T. vaginalis proteins which may stimulate immune responses by human cells.

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참고문헌

  1. Van der Pol B. Trichomonas vaginalis infection: the most prevalent nonviral sexually transmitted infection receives the least public health attention. Clin Infect Dis 2007; 44: 23-25. https://doi.org/10.1086/509934
  2. Lehker MW, Sweeney D. Trichomonad invasion of the mucous layer requires adhesins, mucinases, and motility. Sex Transm Infect 1999; 75: 231-238. https://doi.org/10.1136/sti.75.4.231
  3. Lehker MW, Alderete JF. Iron regulates growth of Trichomonas vaginalis and the expression of immunogenic trichomonad proteins. Mol Microbiol 1992; 6: 123-132. https://doi.org/10.1111/j.1365-2958.1992.tb00844.x
  4. Crouch ML, Alderete JF.Trichomonas vaginalis interactions with fibronectin and laminin. Microbiology 1999; 145: 2835-2843. https://doi.org/10.1099/00221287-145-10-2835
  5. Tsai CD, Liu HW, Tai JH. Characterization of an iron-responsive promoter in the protozoan pathogen Trichomonas vaginalis. J Biol Chem 2002; 277: 5153-5162. https://doi.org/10.1074/jbc.M110234200
  6. Garcia AF, Chang TH, Benchimol M, Klumpp DJ, Lehker MW, Alderete JF. Iron and contact with host cells induces expression of adhesins on surface of Trichomonas vaginalis. Mol Microbiol 2003; 47: 1207-1224. https://doi.org/10.1046/j.1365-2958.2003.03366.x
  7. Peterson KM, Alderete JF. Iron uptake and increased intracellular enzyme activity follow host lactoferrin binding by Trichomonas vaginalis receptors. J Exp Med 1984; 160: 398-410. https://doi.org/10.1084/jem.160.2.398
  8. Lehker MW, Arroyo R, Alderete JF. The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis. J Exp Med 1991; 174: 311-318. https://doi.org/10.1084/jem.174.2.311
  9. Lehker MW, Chang TH, Dailey DC, Alderete JF. Specific erythrocyte binding is an additional nutrient acquisition system for Trichomonas vaginalis. J Exp Med 1990; 171: 2165-2170. https://doi.org/10.1084/jem.171.6.2165
  10. Ardalan S, Lee BC, Garber GE. Trichomonas vaginalis: the adhesin AP51 and AP65 bind heme and hemoglobin. Exp Parasitol 2009; 121: 300-306. https://doi.org/10.1016/j.exppara.2008.11.012
  11. Ryu JS, Choi HK, Min DY, Ha SE, Ahn MH. Effect of iron on the virulence of Trichomonas vaginalis. J Parasitol 2001; 87: 457-460. https://doi.org/10.1645/0022-3395(2001)087[0457:EOIOTV]2.0.CO;2
  12. Kucknoor AS, Mundodi V, Alderete JF. The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65. Cell Microbiol 2007; 9: 2586-2597. https://doi.org/10.1111/j.1462-5822.2007.00979.x
  13. Diamond LS. The estabilishment of various trichomonads of animals and man in axenic cultures. J Parasitol 1957; 43: 488-490.
  14. Moreno-Brito V, Yanez-Gomez C, Meza-Cervantez P, Avila-Gonzalez L, Rodriguez MA, Ortega-Lopez J, Gonzalez-Robles A, Arroyo R. A Trichomonas vaginalis 120 kDa protein with identity to hydrogenosome pyruvate: ferridosin oxidoreductase is a surface adhesion induced by iron. Cell Microbiol 2005; 7: 245-258.
  15. Garcia AF, Alderete JF. Characterization of the Trichomonas vaginalis surface-associated AP65 and binding domain interacting with trichomonads and host cells. BMC Microbiol 2007; 7: 116. https://doi.org/10.1186/1471-2180-7-116
  16. Addis MF, Rappelli P, Delogu G, Carta F, Cappiccinelli P, Fiori PL. Cloning and molecular characterization of cDNA clone coding for Trichomonas vaginalis alpha-actinin and intracellular localization of the protein. Infect Immun 1998; 66: 4924-4931.
  17. Manning BD, Snyder M. Drivers and passengers wanted! The role of kinesin-associated proteins. Trends Cell Biol 2000; 10: 281-289. https://doi.org/10.1016/S0962-8924(00)01774-8
  18. Tucker RP, Chiquet-Ehrismann R. Teneurins: a conserved family of transmembrane proteins involved in intercellular signaling during development. Dev Biol 2006; 290: 237-245. https://doi.org/10.1016/j.ydbio.2005.11.038
  19. O'Brien JL, Lauriano CM, Alderete JF. Molecular characterization of a third malic enzyme-like AP 65 adhesin gene of Trichomonas vaginalis. Microb Pathog 1996; 20: 335-349. https://doi.org/10.1006/mpat.1996.0032
  20. Kim J, Shin MH, Song KJ, Park SJ. Evaluation of $\alpha$-tubulin as an antigenic and molecular probe to detect Giardia lamblia. Korean J Parasitol 2009; 47: 287-291. https://doi.org/10.3347/kjp.2009.47.3.287
  21. Alderete JF, O'Brien JL, Arroyo R, Engbring JA, Musatovova O, Lopez O, Lauriano CM, Nguyen J. Cloning and molecular characterization of two genes encoding adhesion proteins involved in Trichomonas vaginalis cytoadherence. Mol Microbiol 1995; 17: 69-83. https://doi.org/10.1111/j.1365-2958.1995.mmi_17010069.x
  22. Alderete JF, Engbring J, Lauriano CM, O'Brien JL. Only two of the Trichomonas vaginalis triplet AP51 adhesins are regulated by iron. Microb Pathog 1998; 24: 1-16. https://doi.org/10.1006/mpat.1997.0167
  23. Engbring JA, Alderete JF. Three genes encode distinct AP33 proteins involved in Trichomonas vaginalis cytoadherence. Mol Microbiol 1998; 28: 305-313. https://doi.org/10.1046/j.1365-2958.1998.00784.x
  24. Pancholi V, Fischetti VA. Cell-to-cell signaling between group A streptococci and paryngeal cells. Role of streoptococcal surface dehydrogenase (SDH). Adv Exp Med Biol 1997; 418: 499-504.

피인용 문헌

  1. Trichomonas vaginalis α-Actinin 2 Modulates Host Immune Responses by Inducing Tolerogenic Dendritic Cells via IL-10 Production from Regulatory T Cells vol.55, pp.4, 2011, https://doi.org/10.3347/kjp.2017.55.4.375
  2. Role of α-Actinin 2 in Cytoadherence and Cytotoxicity of Trichomonas vaginalis vol.27, pp.10, 2011, https://doi.org/10.4014/jmb.1706.06050