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09:04
Detection of Neu1 Sialidase Activity in Regulating TOLL-like Receptor Activation
Published on: September 7, 2010
Sialic acid-specific lectin from Tritrichomonas foetus
P Babál1, F F Pindak, L C Russell
1Department of Pathology, University of South Alabama, 2451 Fillingim Street, Mobile, AL 36617, USA. pbalal@jaguar1.usouthal.edu
Biochimica Et Biophysica Acta
|June 15, 1999
Summary
A novel sialic acid-specific lectin (TFL) from Tritrichomonas foetus was identified and characterized. This lectin shows potential for diagnosing and preventing bovine trichomoniasis.
Area of Science:
- Microbiology
- Biochemistry
- Parasitology
Background:
- Tritrichomonas foetus is a protozoan parasite causing bovine trichomoniasis.
- Sialic acid-binding lectins play roles in host-parasite interactions.
- Understanding parasite adhesion mechanisms is crucial for disease control.
Purpose of the Study:
- To isolate and characterize a novel sialic acid-specific lectin from T. foetus.
- To investigate the lectin's biochemical properties and substrate specificity.
- To explore the potential diagnostic and therapeutic applications of the lectin.
Main Methods:
- Purification of the lectin (TFL) using erythrocyte adsorption and affinity chromatography.
- Molecular weight determination by gel filtration and SDS-PAGE.
- Characterization of binding specificity using various sialic acid derivatives and hemagglutination inhibition assays.
- Antibody-based detection of TFL on the parasite surface.
Main Results:
- A novel sialic acid-specific lectin (TFL) of 728 kDa was purified from T. foetus.
- TFL is composed of 66 kDa subunits and is glycosylated.
- The lectin binds N-acetyl and N-glycolyl neuraminic acid, with weaker affinity for O-acetylated forms and colominic acid.
- TFL requires no cations, functions optimally at neutral pH, and is stable at 4°C.
- Anti-TFL antibodies confirmed membrane localization, suggesting a role in parasite adhesion.
Conclusions:
- TFL is a novel, stable, and immunogenic sialic acid-binding lectin from T. foetus.
- Its specific binding properties and membrane localization suggest a role in parasite adhesion.
- TFL represents a promising candidate for developing diagnostics and prevention strategies for bovine trichomoniasis.
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