A proteomic approach to the identification of tegumental proteins of male and female Schistosoma bovis worms.
Schistosoma bovis, a parasite of ruminants, can live for years in the bloodstream in spite of the immune response of its host. The parasite tegument covers the entire surface of the worm and plays a key role in the host-parasite relationship. The parasite molecules involved in host immune response evasion mechanisms must be expressed on the tegument surface and are potential targets for immune or drug intervention. The purpose of the present work was to identify the tegumental proteomes of male and female S. bovis worms, in particular the proteins expressed on the outermost layers of the tegument structure. Adult worms of each sex were treated separately with trypsin in order to digest their tegumental proteins, after which the peptides released were analysed by LC-MS/MS for identification. This experimental approach afforded valuable information about the protein composition of the tegument of adult S. bovis worms. A range of tegumental proteins was identified, most of which had not been identified previously in this species. Although an absolute purification of the proteins expressed on the outermost layers of the tegument structure was not achieved, it is likely that present among the proteins identified are some of the molecules most closely associated with the tegument surface. Our study also suggests that there may be differences in the protein composition of the tegument of male and female schistosomes. Finally, the presence of actin and GAPDH on the surface of male and female worms and the presence of enolase exclusively on the surface of male worms were verified by confocal microscopy.
Pérez-Sánchez
Ricardo
R
Parasitology Laboratory, Instituto de Recursos Naturales y Agrobiología de Salamanca (CSIC), Cordel de Merinas 40-52, Salamanca, Spain.
Valero
María Luz
ML
Ramajo-Hernández
Alicia
A
Siles-Lucas
Mar
M
Ramajo-Martín
Vicente
V
Oleaga
Ana
A
D000818:Animals; D005260:Female; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008297:Male; D013058:Mass Spectrometry; D018613:Microscopy, Confocal; D020543:Proteome / Q000378:metabolism; D040901:Proteomics; D012547:Schistosoma / Q000145:classification / Q000378:metabolism* / Q000648:ultrastructure; D014357:Trypsin / Q000378:metabolism
D015801:Helminth Proteins; D020543:Proteome; D014357:Trypsin