Proteomic identification of endothelial cell surface proteins isolated from the hepatic portal vein of mice infected with Schistosoma bovis.

Schistosomes are blood parasites adapted to their intravascular habitat that have evolved mechanisms to evade the immune and hemostatic responses of their hosts. It has been observed that the schistosome can regulate the endothelium function along the infection, which contributes to modulation of host defensive responses and parasite survival. The purpose of this work was the analysis of the changes induced by Schistosoma bovis adult worms in the proteome expressed by infected mice on the endothelial surface of their portal vein. With this aim, we have utilized a methodology that allows the purification, identification and relative quantification of endothelial cell surface proteins after their selective in vivo labeling with biotin. Trypsin digestion of the biotinylated proteins and subsequent liquid chromatography and tandem mass spectrometry analysis (LC-MS/MS) resulted in the identification of a total 127 non-redundant proteins. All these proteins have been classified according to their function and cellular location, and the differences between S. bovis-infected and non-infected mice in their endothelial surface proteomes have been analyzed. The present work provides the first data on the proteome of the endothelial surface of the portal vein, and identifies some of the changes induced in it after an infection by S. bovis.