Abstract
GP300 is a high molecular weight glycoprotein of the bovine lungworm Dictyocaulus viviparus. The N-linked glycans are substituted with phosphorylcholine (PC) giving it immunomodulatory potential. GP300 is highly immunogenic and its recognition by IgE antibodies is correlated with protection against infection. Here we identified and characterized the protein backbone of GP300. Mass spectrometric analysis on purified GP300 and DNA sequencing of the corresponding gene indicated that GP300 is a thrombospondin-like protein with 7 thrombospondin domains, 6 kunitz domains and 15 putative N-glycosylation sites. Purified GP300 display protease inhibitory activity. The protein was located in the brushborder of the gut, but also in muscles, hypodermis and the lining of the uterus. Analysis of GP300 orthologues in Haemonchus contortus and Cooperia oncophora revealed that these proteins also contain PC-substituted N-glycans and showed immunological cross-reactive responses. These data suggest the existence in nematodes of a GP300 protein family that is characterized by PC-substituted N-linked glycans attached to a thrombospondin-like protein backbone. This finding is of particular interest considering the immunomodulatory and vaccine potential of members of the GP300 family.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
