A COMPARISON OF THE PROTEIN PROFILE OF TRIAENOPHORUS NODULOSUS PLEROCERCOIDS FROM DIFFERENT INTERMEDIATE HOSTS

Abstract

The spectrum of proteins was studied in plerocercoids of parasitic cestodes Triaenophorus nodulosus collected from the liver of different species of fish: perch Perca fluviatilis L., ruffe Gymnocephalus cernuus L. and burbot Lota lota L. A comparison of protein extracts separated by 2D electrophoresis revealed 18 proteins whose concentrations differed among larvae of different fish species. Of these, 4 proteins were identified by using mass-spectrometric methods (MALDI-TOF/TOF, LC–MS): a carbohydrate metabolism enzyme triosephosphate isomerase, the proteins of microtubules tubulin α and β, and the G-protein signaling molecule. The elevated content of components of the G-protein pathway of the cytoskeleton and cell morphology regulation (tubulin and G-protein) in plerocercoids from perch in comparison with plerocercoids from burbot indicate a more dynamic cytoskeleton, increased cell proliferation and differentiation processes, and possibly more mature larvae in the former species. A higher level of expression of the key enzyme of glycolysis and signal transmission in plerocercoids from perch compared to plerocercoids from burbot indicates a greater metabolic activity in larvae from perch. The obtained results indicate that the expression of some proteins in T. nodulosus larvae is influenced by the habitat.

Keywords

• proteomics
• helminths
• triaenophorus
• cestoda
• intermediate hosts.