Grafting glycoprotein-derived oligosaccharides structures onto non-glycosylated polypeptides.

Properties of recombinant glycoproteins can be altered by the addition of oligosaccharide structures specific to the cells used for its heterologous expression. A methodology was implemented to obtain a glycopeptide preparation useful to elucidate the role of carbohydrates in the immunogenicity and antigenicity of glycoproteins. It consists on the digestion of the protein, followed by selective capture of the oligosaccharides bound to di-/tripeptides, and their grafting onto a non-glycosylated receptor protein by chemical crosslinking.

Dominant epitopes of cross-reactive anti-domain III human antibody response change from early to late convalescence of infection with dengue virus.

Cross-neutralizing activity of human antibody response against Dengue virus complex (DENV) changes importantly over time. Domain III (DIII) of the envelope protein of DENV elicits a potently neutralizing and mostly type-specific IgG response. We used sera from 24 individuals from early- or late convalescence of DENV1 infection to investigate the evolution of anti-DIII human IgG with the time lapse since the infection.

A time-efficient workflow to purify a library of alanine mutants of surface-exposed residues of the domain III of the envelope protein of dengue virus serotype 1.

Dengue complex is formed by four viral serotypes that cause the disease of the same name. Dengue is the arthropod-borne disease with the highest incidence worldwide. The envelope glycoprotein comprises three structural domains.