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

Abstract

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

In vivo intravascular biotinylation of Schistosoma bovis adult worms and proteomic analysis of tegumental surface proteins

“…It is also worth mentioning that we failed to identify host plasminogen on the tegument despite the fact that this is an abundant plasma protein and that S. bovis can bind plasminogen on its surface [5]. Similarly, in other study in which we applied the same methodology to analyze the proteome of the endothelial surface of the portal vein of naïve mice and mice infected with S. bovis we also failed to detect plasminogen in spite of the presence of plasminogen receptors on the endothelial surface [24]. As a whole, these results seem to suggest that the method used in both studies would not be appropriate to capture and identify this protein.…”

“…The method of vascular perfusion in vivo with sulfo-NHS-LC-biotin has been used in several disease models in order to establish an atlas of vascular proteins in health and disease [29][30][31][32][33]. More recently, we applied this methodology to study the proteome of the endothelial surface of the mouse portal vein, and we identified some of the changes induced in it after infection by S. bovis [24]. The present work is the first in which vascular perfusion has been used to investigate, in vivo, the proteins exposed by an intravascular pathogen on its surface to the host.…”

“…is a stress protein belonging to the HSP70 multigene family that shows 76% identity to its homologous protein identified in the endothelial vascular surface of the portal vein of S. bovis-infected mice [24]. The expression of this protein in the vascular endothelium has an inhibitory effect on coagulation through the regulation of tissue factor [40], such that it is possible that the GRP78 expressed on the S. bovis tegument might have a similar function.…”

“…bovis tegument we found some proteins that had never been identified on the schistosome surface, such as several blood components (Apolipoprotein, transferrin, a serine protease inhibitor and fibrinogen in great abundance) and proteins from the host endothelial vascular surface (basigin, dipeptidil peptidase, and vitronectin). The presence of these last proteins on the surface of S. bovis reflects the intimate contact of the parasite with endothelia during intravascular movement [24]. We believe that one reason for failing to identify these proteins at the surface of the tegument in the in vitro studies would be that they may be easily lost during the washings and manipulations to which the parasites were subjected.…”

Development of a strategy for the identification of surface proteins in the pathogenic microsporidianNosema bombycis

“…However, we cannot ignore that the different protein extraction methods used in the current and previous research might account for the distinct protein libraries obtained, resulting in 8 other hypothetical proteins not being present in our LC-MS/MS data. Additionally, the level of expression of the remaining proteins on the spore surface might be too low to be detected, being masked by other much more abundant surface proteins (Arjunan et al 2009; de la Torre-Escudero et al 2012). Finally, the extracellular domains of the 8 putative proteins exposed on the spore surface likely cannot be biotinylated because they lack the ε-amine of lysine residues (de la Torre-Escudero et al 2012).…”