Effect of O-linked glycosylation on the antigenicity, cellular uptake and trafficking in dendritic cells of recombinant Ber e 1

Ber e 1, a major Brazil nut allergen, has been successfully produced in the yeast Pichia pastoris expression system as homogenous recombinant 1 (rBer 1) with similar physicochemical properties and identical immunoreactivity to its native counterpart, nBer 1. However, O -linked glycans was detected on P . -derived rBer which is not naturally present may contribute allergic sensitisation. In this study, we addressed glycosylation differences between counterparts. We also determined whether fungal could affect antigenicity immunogenicity of by using dendritic cells (DC) an immune cell model due their role modulating response. identified that occurs at Ser96, Ser101 Ser110 large chain Ser19 small polypeptide only. The shown elicit varying degree binding different combination human leukocyte antigens (HLA) frequencies compared when tested DC-T assay. both forms are weak immunogens based from low response indexes (RI). Glycans were increase efficiency protein recognition internalization murine bone marrow-derived (bmDC) via C-type lectin receptors, particularly mannose receptor (MR), non-glycosylated SFA8, allergenic 2S albumin sunflower seed. Binding glycosylated MR alone found induce production IL-10 modulates bmDC polarise Th2 suppressing IL-12 DC maturation. Our findings suggest but measurable effect vitro thus influence applications diagnostics immunotherapy.