6533b7d7fe1ef96bd1267a86

RESEARCH PRODUCT

Specific tyrosine phosphorylation in response to bile in Fasciola hepatica and Echinostoma friedi

Antonio MarcillaInés CarpenaJosé Guillermo EstebanRafael ToledoAna EspertJosé Enrique De La Rubia

subject

ImmunologyBile Acids and Saltschemistry.chemical_compoundCricetinaeEchinostomaparasitic diseasesAnimalsFasciola hepaticaParasite hostingPhosphorylationTyrosinebiologyHost (biology)Tyrosine phosphorylationGeneral MedicineFasciola hepaticabiology.organism_classificationInfectious DiseaseschemistryBiochemistryTyrosinePhosphorylationCattleParasitologyTrematodaEchinostoma

description

Protein tyrosine phosphorylation (PY) is a well-known signalling mechanism which is also involved in host-parasite interactions. Despite its transcendence, PY has been poorly studied in parasitic helminths. The aim of this study is to examine the effect of bile salts on the PY pattern in parasitic trematodes. Two distinct adult models were analysed: Echinostoma friedi, of intestinal habitat, and Fasciola hepatica, naturally inhabitant of host biliary channels. Our results show that bile salts induce specific and distinct protein PY in both trematode species, indicating that this signalling process seems to be also involved in host-trematode relationships.

yearjournalcountryeditionlanguage
2003-10-08Experimental Parasitology
https://doi.org/10.1016/j.exppara.2004.01.006