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Trypanosoma cruzi: a specific surface marker for the amastigote form
M F Lima1, L A Beltz, F Kierszenbaum
1Department of Microbiology and Public Health, Michigan State University, East Lansing 48824-1101.
The Journal of Protozoology
|February 1, 1988
Summary
Trypanosoma cruzi amastigotes bind lactoferrin (LF), a neutrophil glycoprotein. This specific binding, observed on amastigotes but not other forms, suggests a role in parasite-host interactions.
Area of Science:
- Parasitology
- Immunology
- Molecular Biology
Background:
- Trypanosoma cruzi is a protozoan parasite causing Chagas disease.
- Lactoferrin (LF) is an iron-binding glycoprotein with antimicrobial properties.
- Understanding parasite-host interactions is crucial for developing therapeutic strategies.
Purpose of the Study:
- To investigate the interaction between Trypanosoma cruzi life cycle stages and lactoferrin.
- To identify specific parasite surface markers involved in host interactions.
Main Methods:
- Indirect immunofluorescence assays were used to detect LF binding.
- Analysis was performed on amastigotes from various sources (mice, cell culture, axenic medium).
- Comparison of LF binding across different T. cruzi life cycle stages (trypomastigotes, metacyclics, epimastigotes).
Main Results:
- Only Trypanosoma cruzi amastigotes demonstrated binding to lactoferrin.
- LF binding was consistently observed on amastigotes regardless of their origin.
- No LF binding was detected on trypomastigotes, metacyclics, or epimastigotes.
- Increased serum LF levels and surface-bound LF were observed on amastigotes from infected mice spleens.
Conclusions:
- Lactoferrin binding serves as a specific marker for Trypanosoma cruzi amastigotes.
- The amastigote LF receptor may play a significant role in parasite-host interactions, potentially involving mononuclear phagocytes.
- This is the first described naturally occurring ligand for a T. cruzi amastigote surface receptor.