Lectin-binding sites in the midgut of the mosquitoes Anopheles stephensi Liston and Aedes aegypti L. (Diptera: Culicidae).
The presence and distribution of binding sites for eight different lectins, Con A, DBA, HPL, LFA, RCA I, SBA, UEA I, and WGA, were compared in the midguts of Plasmodium gallinaceum-infected Aedes aegypti and Plasmodium berghei-infected Anopheles stephensi. Lectins with high specificity for N-acetyl-D-glucosamine (GlcNAc) exhibited high binding preference for the peritrophic membrane and microvillar glycocalyx of Ae. aegypti; the same structures were preferentially labeled by N-Acetyl-D-galactosamine (GalNAc)-specific lectins in An. stephensi. No differences could be observed in the lectin-binding patterns of the intercellular spaces or cellular organelles and structures. The Plasmodium ookinete surface did not react with any of the lectins tested. It appears that sugars are involved in vector recognition by the parasite and that the peritrophic membrane and/or glycocalyx may be crucial structures for the penetration of the gut epithelium by the ookinete.
Rudin
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W
Schweizerisches Tropeninstitut, Basel, Switzerland.
Hecker
H
H
D000330:Aedes / Q000378:metabolism / Q000469:parasitology* / Q000648:ultrastructure; D000818:Animals; D000852:Anopheles / Q000378:metabolism / Q000469:parasitology* / Q000648:ultrastructure; D001665:Binding Sites; D005110:Extracellular Space / Q000378:metabolism; D005260:Female; D006023:Glycoproteins / Q000378:metabolism; D007150:Immunohistochemistry; D007303:Insect Vectors / Q000378:metabolism / Q000469:parasitology* / Q000648:ultrastructure; D037102:Lectins / Q000032:analysis / Q000378:metabolism*; D008854:Microscopy, Electron; D008871:Microvilli / Q000378:metabolism; D015388:Organelles / Q000378:metabolism; D010961:Plasmodium / Q000502:physiology*; D010962:Plasmodium berghei / Q000502:physiology; D010964:Plasmodium gallinaceum / Q000502:physiology; D011134:Polysaccharides / Q000378:metabolism
D006023:Glycoproteins; D037102:Lectins; D011134:Polysaccharides