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Characterization of binding specificity anti‐glycan monoclonal antibody, L6B8, generated from splenocytes of Schistosoma mansoni‐infected mice

The major antibody responses of humans and animals infected with parasitic flatworms, Schistosoma mansoni, are directed against glycan epitopes of the parasites' glycoconjugates. To facilitate the study of the immunogenic glycan antigens and their role in parasite development, we have used splenocytes from Swiss Webster mice, infected for 11 wk with S. mansoni, to generate hybridomas that secrete monoclonal antibodies to glycan epitopes of the parasites' glycoconjugates. We now report the characterization of the glycan epitope recognized by one of the monoclonal antibodies, L6B8. L6B8 was found to an IgG and it bound to the egg extract in periodate sensitive fashion, indicating the epitope recognized by the monoclonal antibody was glycan in nature. Analysis by ELISA using defined schistosome glycan antigens and also on a glycan array of 442 different glycan structures showed that L6B8 bind to fucosylated lacdiNAc (LDNF; GalNAcβ1–4(Fuc) 1 □1‐3GlcNAc‐R) glycan epitope. We observed by Western blot analysis and immunostaining of life cycle stages of S. mansoni using L6B8 that the epitope is highly expressed by adult schistosomes but sparingly expressed by larval and juvenile stages of the parasite. Taken together, our studies show that monoclonal antibody L6B8 is an IgG antibody that specifically binds LDNF glycans and can be used to study the role of LDNF glycans in host –schistosome interactions.