Glycosylation profile of the recombinant BVDV glycoprotein E2 expressed in tobacco callus cultures

ANABELA M. CUTINE; PATRICIA L. MARCONI; GABRIEL A. RABINOVICH; MARIA ALEJANDRA ALVAREZ; KARINA MARIÑO

Capital Federal

Simposio; Primer Simposio Argentino de Glicobiologia GlycoAR 2014; 2014

IFIBINE/FIL/IBYME

Bovine Viral Diarrhea (BVD) is a widespread disease that causes serious mucosal lesions and other clinical manifestations in cattle, with a negative economic impact. The glycoprotein E2 is the major target of the protective immune response against the BVD virus (BVDV) infection, and could potentially be used as a vaccine against the disease. We have established tobacco recombinant in vitro cultures that express variants of the truncated protein E2 (tE2): two recombinant lines were used, one of them with a C-terminal protein tag (KDEL), an endoplasmic reticulum (ER) retention signal which increases the expression level of proteins in transgenic tobacco. Using these tobacco extracts we have confirmed that they exert a protective immune response in guinea pigs. As the biological activity of many glycoproteins relies on their glycosylation profile, and that modifications in the processing of complex glycans in the Golgi apparatus differ between plants and mammals, we have applied different approaches to characterize the glycan structures present in these recombinant E2 forms. Identifying the glycosylation pattern of the recombinant E2 glycoprotein is critical in defining its immunogenicity and might be useful for the development of effective vaccines.