This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mundodi, V.
Right arrow Articles by Alderete, J. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mundodi, V.
Right arrow Articles by Alderete, J. F.

 Previous Article  |  Next Article 

Infection and Immunity, February 2008, p. 523-531, Vol. 76, No. 2
0019-9567/08/$08.00+0     doi:10.1128/IAI.01352-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Immunogenic and Plasminogen-Binding Surface-Associated {alpha}-Enolase of Trichomonas vaginalis{triangledown}

V. Mundodi, A. S. Kucknoor, and J. F. Alderete*

Department of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, Texas 78229-3900

Received 8 October 2007/ Returned for modification 10 November 2007/ Accepted 19 November 2007

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 {alpha}-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 plasminogen-binding {alpha}-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 {varepsilon}-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, surface-associated glycolytic enzyme of T. vaginalis.

* Corresponding author. Present address: School of Molecular Biosciences, Washington State University, P.O. Box 644660, Pullman, WA 99164-4660. Phone: (509) 335-8724. Fax: (509) 335-1949. E-mail: alderete{at}wsu.edu

{triangledown} Published ahead of print on 10 December 2007.

Editor: W. A. Petri, Jr.

Infection and Immunity, February 2008, p. 523-531, Vol. 76, No. 2
0019-9567/08/$08.00+0     doi:10.1128/IAI.01352-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lama, A., Kucknoor, A., Mundodi, V., Alderete, J. F. (2009). Glyceraldehyde-3-Phosphate Dehydrogenase Is a Surface-Associated, Fibronectin-Binding Protein of Trichomonas vaginalis. Infect. Immun. 77: 2703-2711 [Abstract] [Full Text]  
  • Donofrio, F. C., Calil, A. C. A., Miranda, E. T., Almeida, A. M. F., Benard, G., Soares, C. P., Veloso, S. N., Soares, C. M. d. A., Mendes Giannini, M. J. S. (2009). Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein. J Med Microbiol 58: 706-713 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»