Premium
Binding of Lectins to Culture and Vector Forms of Trypanosoma rangeli Tejera, 1920 (Protozoa, Kinetoplastida) and to Structures of the Vector Gut
Author(s) -
RUDIN W.,
SCHWARZENBACH M.,
HECKER H.
Publication year - 1989
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1989.tb01091.x
Subject(s) - biology , hemolymph , lectin , agglutinin , midgut , protozoa , rhodnius prolixus , trypanosoma , pisum , biochemistry , microbiology and biotechnology , botany , virology , insect , larva
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 μg/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.