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ABSTRACT: Objective
To better understand the mechanisms of autoantibodies to the axonal protein contactin-associated protein-like 2 (Caspr2) by studying their target epitopes.Methods
A plasmid for expressing Caspr2 was modified so that the various extracellular subdomains were deleted individually and in groups. Cultured cells were transfected to express these constructs and assayed by immunofluorescence staining with a commercial Caspr2 antibody and a panel of patient sera known to react with Caspr2. Western blotting was also performed. The role of glycosylation in immunogenicity was tested with tunicamycin and PNGase F treatment.Results
Patient antibodies bound to the extracellular domain of Caspr2. Neither native protein structure nor glycosylation was required for immunor
SUBMITTER: Olsen AL
PROVIDER: S-EPMC4496632 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature