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Properties of a blood-meal-induced midgut lectin from the tsetse flyGlossina morsitans
- Source :
- Parasitology Research. 81:271-275
- Publication Year :
- 1995
- Publisher :
- Springer Science and Business Media LLC, 1995.
-
Abstract
- The properties of a blood-meal-induced lectin (agglutinin) from the midgut of Glossina morsitans capable of agglutinating Trypanosoma brucei were studied in vitro. The midgut homogenate from flies that had been fed twice had the highest agglutination activity, followed by that from the once-fed flies and that from the unfed insects. As compared with the bloodstream-form trypanosomes, a much lower concentration of the midgut homogenate was required for agglutination of the procyclic parasites. Furthermore, the agglutination process was specifically inhibited by D-glucosamine. Soybean trypsin inhibitor abrogated agglutination of the bloodstream-form parasites, whereas the procyclics were unaffected. The agglutination process was temperature-sensitive, with little activity being evident between 4 degrees and 15 degrees C. Similarly, heating the midguts to 60 degrees-100 degrees C led to loss of activity. When the midgut homogenate was separated by anion-exchange chromatography, the agglutination activity co-eluted with trypsin activity at approximately 50% NaCl. These results suggest a very close relationship between midgut trypsin-like enzyme and the agglutinin. Since successful agglutination of bloodstream-form trypanosomes requires protease activity, it may be that the enzyme cleaves off some surface molecules on the parasite surface, thus exposing the lectin-binding sites.
- Subjects :
- Male
Tsetse Flies
medicine.medical_treatment
Trypsin inhibitor
Trypanosoma brucei brucei
Biology
Host-Parasite Interactions
Microbiology
Agglutinin
Agglutination Tests
Lectins
Direct agglutination test
medicine
Animals
Rats, Wistar
Glucosamine
Protease
General Veterinary
Kunitz STI protease inhibitor
fungi
Temperature
Midgut
General Medicine
Trypsin
Insect Vectors
Rats
Agglutination (biology)
Infectious Diseases
Biochemistry
Insect Science
Insect Proteins
Parasitology
Trypsin Inhibitors
medicine.drug
Subjects
Details
- ISSN :
- 14321955 and 00443255
- Volume :
- 81
- Database :
- OpenAIRE
- Journal :
- Parasitology Research
- Accession number :
- edsair.doi.dedup.....c8cb24e06f613c2a3ab33357e806416d