Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 144 (1998), 3011-3018
This Article
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 Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Engbring, J. A.
Right arrow Articles by Alderete, J. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Engbring, J. A.
Right arrow Articles by Alderete, J. F.
Agricola
Right arrow Articles by Engbring, J. A.
Right arrow Articles by Alderete, J. F.

microbiology, Vol 144, 3011-3018, Copyright © 1998 by Society for General Microbiology

ARTICLES

Characterization of Trichomonas vaginalis AP33 adhesin and cell surface interactive domains

JA Engbring and JF Alderete
Department of Microbiology, The University of Texas Health Science Center, San Antonio 78284-7758, USA.

Adherence to host target cells is a critical step in establishing infection with the sexually transmitted pathogen Trichomonas vaginalis. Four parasite surface proteins mediating attachment to vaginal epithelial cells have been identified. One surface protein, termed AP33, was characterized further to identify domains interactive with previously generated antibodies and with host surface sites. N- and C- terminal deletion subclones were generated and tested for reactivity with both mAb and rabbit antiserum against AP33, and were also examined for their ability to bind to host cells. Surprisingly, the rabbit antiserum known to inhibit cytoadherence recognized an epitope(s) contained within 72 residues in the N-terminal half of the protein. However, the mAb epitope was immunoreactive with a 28-amino-acid region near the C-terminus. Subsequent mapping of this region with overlapping peptides identified a nine-amino-acid sequence reactive with the mAb. Equally surprising, two domains interactive with host cell surfaces were identified at distinct parts of AP33: one in the N-terminal half of the protein, and the other within 24 residues in the C-terminal third. Further analysis of the C-terminal binding domain revealed that a peptide representing this area could inhibit T. vaginalis cytoadherence by 40%.


This article has been cited by other articles:


Home page
 Infect. Immun.Home page
V. Mundodi, A. S. Kucknoor, and J. F. Alderete
Immunogenic and Plasminogen-Binding Surface-Associated {alpha}-Enolase of Trichomonas vaginalis
Infect. Immun., February 1, 2008; 76(2): 523 - 531.
[Abstract] [Full Text] [PDF]

Home page
 Clin. Microbiol. Rev.Home page
J. R. Schwebke and D. Burgess
Trichomoniasis
Clin. Microbiol. Rev., October 1, 2004; 17(4): 794 - 803.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1998 Society for General Microbiology.