Equilibrium in lung schistosomula sphingomyelin breakdown and biosynthesis allows very small molecules, but not antibody, to access proteins at the host-parasite interface.

The mechanism by which lung-stage schistosomula expose proteins at the host-parasite interface to nutrient, but not antibody, uptake has been obscure. We have found that Schistosoma mansoni and Schistosoma haematobium larvae emerging from host lung at a pH of around 7.5, and fixed with diluted formaldehyde (HCHO), readily bind specific antibodies in indirect membrane immunofluorescence. Data on inhibitors and activators of parasite tegument-bound, magnesium-dependent, neutral sphingomyelinase (nSMase), and sphingomyelin biosynthesis inhibitors revealed that equilibrium in schistosomular sphingomyelin breakdown and biosynthesis prevents antibody binding, yet permits access of small HO-CH2-OH polymers to interact with and cross-link proteins at the host-parasite interface, allowing for their serological visualization.