Journal article
Immunogenic and Plasminogen-Binding Surface-Associated α-Enolase of Trichomonas vaginalis
Infection and immunity, Vol.76(2), pp.523-531
02/2008
Handle:
https://hdl.handle.net/2376/115597
PMCID: PMC2223476
PMID: 18070902
Abstract
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 α-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 α-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 ɛ-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
.
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Details
- Title
- Immunogenic and Plasminogen-Binding Surface-Associated α-Enolase of Trichomonas vaginalis
- Creators
- V Mundodi - Department of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, Texas 78229-3900A. S Kucknoor - Department of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, Texas 78229-3900J. F Alderete - Department of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, Texas 78229-3900
- Publication Details
- Infection and immunity, Vol.76(2), pp.523-531
- Academic Unit
- Molecular Biosciences, School of
- Publisher
- American Society for Microbiology (ASM)
- Identifiers
- 99900547977401842
- Language
- English
- Resource Type
- Journal article