Abstract
DENV envelope glycoprotein (E) is responsible for interacting with host cell receptors and is the main target for the development of a dengue vaccine based on an induction of neutralizing antibodies. It is well known that DENV E glycoprotein has two potential N-linked glycosylation sites at Asn67 and Asn153. The N-glycans of E glycoprotein have been shown to influence the proper folding of the protein, its cellular localization, its interactions with receptors and its immunogenicity. However, the precise structures of the N-glycans that are attached to E glycoprotein remain elusive, although the crystal structure of DENV E has been determined. This study characterized the structures of envelope protein N-linked glycans on mature DENV-2 particles derived from insect cells via an integrated method that used both lectin microarray and MALDI-TOF-MS. By combining these methods, a high heterogeneity of DENV N-glycans was found. Five types of N-glycan were identified on DENV-2, including mannose, GalNAc, GlcNAc, fucose and sialic acid; high mannose-type N-linked oligosaccharides and the galactosylation of N-glycans were the major structures that were found. Furthermore, a complex between a glycan on DENV and the carbohydrate recognition domain (CRD) of DC-SIGN was mimicked with computational docking experiments. For the first time, this study provides a comprehensive understanding of the N-linked glycan profile of whole DENV-2 particles derived from insect cells.
Highlights
Dengue virus (DENV) is the most important arthropod-borne human pathogen that is transmitted by the Aedes aegypti mosquito in tropical and subtropical countries[1]
We characterized the N-glycan profile of the surface of DENV-2 derived from insect cells
N-glycan structures were solved from purified DENV-2 virions by combining lectin microarray with MALDI-TOF-MS
Summary
Dengue virus (DENV) is the most important arthropod-borne human pathogen that is transmitted by the Aedes aegypti mosquito in tropical and subtropical countries[1]. N-Glycosylation Pattern of Insect Derived Mature Dengue 2 Virus hemorrhagic fever (DHF) cases[2]. There are four genetically related DENV serotypes, and it is believed that DHF may result from secondary infection with different virus serotypes in which antibody-mediated disease enhancement (ADE) is involved[3]. This feature makes developing a DENV vaccine very difficult because an effective vaccine must successfully protect people against all four virus serotypes. Understanding the structure and function of the viral surface glycoprotein can be helpful in designing potent immunogens that safely protect against disease[4]
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