Three radiolabeled substances were mixed with fresh heparinized mouse blood and fed to female Anopheles stephensi through a chicken crop membrane. Resorption and transport in the anterior (A) and posterior (P, stomach) parts of the midgut were investigated by means of electron microscopic autoradiography. Digestion products of 125I-labeled bovine serum albumin (BSA) were resorbed only in the P-part, showing a biphasic pattern with maximal values 4 and 18 hr after feeding. Uptake of 3H-labeled amino acids started immediately after feeding in both midgut parts. [14C]glucose was mainly absorbed in the P-part. Labeled carbohydrate storage deposits formed during the initial phase of digestion and were mobilized around 36 hr after feeding. After feeding the mosquitoes on 125I-BSA, oocyte protein yolk spheres and abdominal cuticle became labeled. Ingestion of 3H-labeled amino acids caused the formation of silver grains over follicles and fat body lipids. Feeding on [14C]glucose resulted in labeled fat body carbohydrates and oocyte protein yolk spheres.

Animals↗

PubMedDate not supplied

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

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.

Agglutination Tests↗