Protein and lipoprotein uptake by developing oocytes of the hawkmoth Manduca sexta. An ultrastructural and immunocytochemical study.

The ultrastructure of developing Manduca sexta oocytes is described with respect to the endocytic pathway for protein incorporation. Three major (lipo) protein components of mature M. sexta eggs, lipophorin, vitellogenin and microvitellogenin, were localized along this pathway by immuno-fluorescence and immuno-gold labeling techniques. Labeling of the antigens was observed in the extracellular spaces of the follicle. In those cases where fixation and en bloc staining procedures did not destroy antigenicity, antigens were detected in coated pits and coated vesicles near the plasma membrane of the oocyte. All three antigens were demonstrated to be present in endosomes in the cortex of the oocyte. Both the morphology and the labeling pattern of the endosomes indicate that this organelle is a compartment of uncoupling of receptor and ligand. Tubular elements at the surface of the endosome, interpreted to be involved in the recycling of receptors and membrane to the oocyte surface, were not labeled. Strong labeling of lipophorin, vitellogenin and microvitellogenin was observed in the developing yolk bodies, the main protein storage compartment of the oocyte. The uptake and storage of hemolymph proteins and lipoproteins by M. sexta oocytes is discussed in comparison with other insect and vertebrate endocytic systems.