Lipid and membrane protein transfer from human neutrophils to schistosomes is mediated by ligand binding.

Attachment of human neutrophils to schistosomula of Schistosoma mansoni involves leukocyte receptors recognizing carbohydrate, complement and/or IgG ligands on the parasite surface. Here, we examined the transfer of a fluorescent fatty acid analog (BOFA) from human neutrophils to schistosomula coated with concanavalin A (Con A), immune serum or nonimmune serum under co-culture conditions by fluorescence confocal laser scanning microscopy (CLSM). Coating schistosomes with Con A or immune serum and co-culturing them for 24 hours with BOFA-labeled neutrophils resulted in a specific lipid transfer to the surface tegument of the schistosomes. Tegumental labeling was absent when nonimmune serum was used. No significant difference (P < 0.001) was found in the number of neutrophils bound to the worm surface between Con A-coated schistosomes (4.1 +/- 0.345 cells/worm) and worms incubated in immune serum (4.261 +/- 0.362). The number of neutrophils bound to the schistosomula (2.7 +/- 0.223) was significantly reduced in the presence of nonimmune serum (P < 0.0001). The viability of the schistosomula was 98% in nonimmune treated co-cultures, and 91% in cocultures treated with immune serum. HPLC analysis of labeled neutrophils demonstrated that BOFA was incorporated into both phospholipids and neutral lipids, which were almost exclusively triglycerides and, after 18 hours of culture, all of the fatty acid analog was incorporated into complex lipids. Double-label experiments in which schistosomula bearing Con A were first incubated with BOFA-labeled neutrophils and subsequently immunolabeled revealed that the neutrophil membrane proteins, MHC class I, CR1 and CR3 were co-transferred with neutrophil lipids to the parasite tegument.(ABSTRACT TRUNCATED AT 250 WORDS)