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Published on: October 1, 2015
Lactoferrin-binding proteins of Tritrichomonas foetus
D J Grab1, J D Lonsdale-Eccles, M W Oli
1Department of Parasitology, Kurume University School of Medicine, Fukuoka, Japan.
The Journal of Parasitology
|November 7, 2001
Summary
Tritrichomonas foetus, a cattle parasite, requires iron from lactoferrin. Researchers identified potential lactoferrin-binding proteins on the parasite, suggesting specific interactions and fragmentation may be involved in iron acquisition.
Area of Science:
- Parasitology
- Molecular Biology
- Biochemistry
Background:
- Tritrichomonas foetus is a significant protozoan parasite affecting cattle reproduction.
- Iron acquisition from host lactoferrin is crucial for T. foetus survival.
- Specific lactoferrin-binding proteins in T. foetus remain unidentified.
Purpose of the Study:
- To identify and characterize lactoferrin-binding proteins in T. foetus.
- To differentiate specific and non-specific lactoferrin binding mechanisms.
- To investigate factors influencing lactoferrin-T. foetus interactions.
Main Methods:
- Lactoferrin affinity chromatography and Western blotting were employed.
- Proteins were metabolically or surface-labeled for detection.
- Competitive inhibition studies and SDS-PAGE were utilized.
Main Results:
- Bovine lactoferrin exhibited higher binding affinity to T. foetus than human lactoferrin or bovine transferrin.
- Specific binding was predominant, but non-specific, charge-related interactions were also observed.
- SDS-PAGE identified potential lactoferrin-binding proteins at 22, 49, 55, 72, and 155 kDa.
Conclusions:
- The 155 kDa protein is a candidate for the specific lactoferrin receptor, with lower molecular weight proteins possibly being fragments.
- Lactoferrin binding is likely regulated by a combination of specific receptor interactions and non-specific forces.
- Bovine cervical mucus can diminish lactoferrin binding to T. foetus.
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