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Binding of lectins to culture and vector forms of Trypanosoma rangeli Tejera, 1920 (Protozoa, Kinetoplastida) and to structures of the vector gut.

Authors
  • Rudin, W
  • Schwarzenbach, M
  • Hecker, H
Type
Published Article
Journal
The Journal of protozoology
Publication Date
Jan 01, 1989
Volume
36
Issue
6
Pages
532–538
Identifiers
PMID: 2689636
Source
Medline
License
Unknown

Abstract

Culture forms of Trypanosoma rangeli could be agglutinated with Canavalia ensiformis (Con A) lectin and, less effectively with Pisum sativum agglutinin (PEA), at a concentration of 200 micrograms/ml. Ricinus communis agglutinin I (RCA I) agglutinated trypanosomes only if they were not previously washed with physiological Ringer's solution. Three other lectins did not react with the same parasite forms. Direct or indirect lectin-gold labeling techniques were applied to LR-White embedded thin sections of T. rangeli culture forms and to forms in the gut, hemolymph, and salivary glands of Rhodnius prolixus. Under these conditions, Con A was the only lectin out of 9 that bound to the surface of trypanosomes from culture and from the bug hemolymph. Con A did not react with any midgut or salivary gland forms. The preservation of the biological activity of the lectin-gold complexes that did not bind to the parasite surface was confirmed by reactions with structures of the invertebrate host.

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