Abstract
Parasitic helminths of the genus Schistosoma synthesize an assortment of glycoconjugates with unique glycan structures that play immuno‐modulatory role(s) in host‐parasite interactions. The unique feature of schistosome glycans is the presence of LacdiNAc (LDN; GalNAcâ1‐4GlcNAC‐) outer branches instead of the lactosamine (LN; Galâ1‐4GlcNAC‐) branches associated with mammalian glycoconjugates. IgM and IgG antibodies are generated to LDN epitopes during course of schistosome infections in vertebrates. We report the use of splenocytes from Schistosoma mansoni infected Swiss Webster mice to generate IgG monoclonal antibodies to LDN epitope to facilitate the study of the role of LDN antigen in host‐schistosome interactions. Splenocytes were prepared from spleens harvested from Swiss Webster mice at wk 10 post‐infection and fused with myeloma cells to generate hybridomas. The secreted monoclonal antibody Y1H5 was purified over columns of MEP‐hypercel and its specificity for LDN epitopes was analyzed on the glycan array of the Consortium for Functional Glycomics against 660 different glycan structures. The availability of anti‐LDN monoclonal antibody would allow the purification and localization of LDN epitopes during parasite development in intermediate and mammalian hosts.
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.
