Background: Parasites secrete and excrete a variety of molecules evolve to help establish and sustain infections within hosts. Parasite adaptation to their host may lead to between-population divergence in these excretory and secretory products (ESPs), but few studies have tested for intraspecific variation in helminth proteomes.
Methods: Schistocephalus solidus is a cestode that parasitizes three spined stickleback, Gasterosteus aculeatus . We used an ultra-performance liquid chromatography-mass spectrometry protocol to characterize the ESP and whole-body proteome of S. solidus. Specifically, we characterized the proteome of S. solidus at the plerocercoid stage from wild caught stickleback from three lakes on Vancouver Island (British Columbia, Canada) and one lake in Alaska (United States). We tested for differences in proteome composition among the four populations and specifically between ESPs and body tissue.
Results: Overall, we identified 1362 proteins in the total proteome of S. solidus, with 542 of the 1362 proteins detected exclusively in the ESPs. Of the ESP proteins, we found signaling peptides and transmembrane proteins that were previously not detected or characterized in S. solidus. We also found protein spectrum counts greatly varied between all lake populations.
Conclusions: These population-level differences were observed in both ESP and tissue types. Our study suggests that S. solidus can excrete and secrete a wide range of proteins which are distinct among populations. These differences might reflect plastic responses to host genotype differences, or evolved adaptations by Schistocephalus to different local host populations.