Abstract

Schistosoma bovis is a parasite of ruminants that causes significant economic losses to farmers throughout Africa, Southwestern Asia and the Mediterranean. Additionally, recent studies have reported its zoonotic potential through the formation of S. bovis×Schistosoma haematobium hybrids. As observed in the Schistosoma species infecting humans, it is assumed that S. bovis has also evolved host regulatory molecules that ensure its long-term survival in the bloodstream of its host. Since these molecules could be potential targets for the development of new drugs and anti-schistosome vaccines, their identification and functional characterization were undertaken.With this aim in mind, the molecular interface between S. bovis and its vertebrate host was subjected to a series of proteomic studies, which started with the analysis of the proteomes of the S. bovis moieties exposed to the host, namely, the excretory/secretory products and the tegument surface. Thus, a wealth of novel molecular information of S. bovis was obtained, which in turn allowed the identification of several parasite proteins with fibrinolytic and anticoagulant activities that could be used by S. bovis to regulate the host defensive systems.Following on, the host interface was investigated by studying the proteome of the host vascular endothelium surface at two points along the infection: in the lung vessels during the schistosomula migration and in the portal vein after the parasites have reached adulthood and sexual maturity. These studies have provided original data regarding the proteomes of the endothelial cell surface of pulmonary vasculature and portal vein in S. bovis-infected animals, and have shown significant changes in these proteomes associated with infection.This review compiles current information and the analyses of all the proteomic data from S. bovis and the S. bovis-host interface, including the molecular and functional characterization of S. bovis proteins that were found to participate in the regulation of the host coagulation and fibrinolysis systems.

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