Glycosylation of viral proteins: Implication in virus–host interaction and virulence

Abstract

Glycans are among the most important cell molecular components. However, given their structural diversity, their functions have not been fully explored. Glycosylation is a vital post-translational modification for various proteins. Many bacteria and viruses rely on N -linked and O-linked glycosylation to perform critical biological functions. The diverse functions of glycosylation on viral proteins during viral infections, including Dengue, Zika, influenza, and human immunodeficiency viruses as well as coronaviruses have been reported. N -linked glycosylation is the most common form of protein modification, and it modulates folding, transportation and receptor binding. Compared to N -linked glycosylation, the functions of O-linked viral protein glycosylation have not been comprehensively evaluated. In this review, we summarize findings on viral protein glycosylation, with particular attention to studies on N-linked glycosylation in viral life cycles. This review informs the development of virus-specific vaccines or inhibitors.

The replication properties of a contemporary Zika virus from West Africa depends on NS1/NS4B proteins

“…We wondered whether a specific part of genomic viral RNA might play a role in attenuated replication of GUINEA-18 in vitro . The GUINEA-18 structural proteins with the N-glycosylated E protein may have an effect on virus binding efficiency in decreasing the host-cell susceptibility to viral infection (26,27). The importance of 5’ region of GUINEA-18 in viral attenuation was examined using GUINEA-18/MR766 5’region chimera in which the 5’NCR followed by the sequence coding for C, prM and E proteins of GUINEA-18 were replaced by the counterpart region of MR766 MC using genetic reverse experiments based on ISA method (Fig.…”

A Synergistic Lipid Nanoparticle Encapsulating mRNA Shingles Vaccine Induces Potent Immune Responses and Protects Guinea Pigs from Viral Challenges

“…[45] Recent studies have indicated that modifications to the glycosylation pattern of viral antigens can impact their interaction with antibodies and subsequently influence immune responses. [46,47] Nordén et al demonstrated that reducing interfering O-linked glycans on the gE protein of VZV could enhance its binding to IgG antibodies, potentially leading to improved immune recognition and response. [48] To investigate whether modifying the glycosylation pattern of VZV gE could induce stronger immune responses, three mRNA sequences were designed and synthesized.…”

Effective Infection with Dengue Virus in Experimental Neonate and Adult Mice through the Intranasal Route

“…Viruses are obligate intracellular infectious agents that exploit host machinery to modify their viral proteins for survival. One of the key modifications is protein glycosylation [ 32 ]. As the secreted viruses are restricted in semisolid medium, the plaque forming must rely on the virus mediated cell-cell membrane fusion, which could be affected by the glycosylation modifications of virus [ 32 ].…”

“…One of the key modifications is protein glycosylation [ 32 ]. As the secreted viruses are restricted in semisolid medium, the plaque forming must rely on the virus mediated cell-cell membrane fusion, which could be affected by the glycosylation modifications of virus [ 32 ]. Therefore, we hypothesized that the glycosylation modifications level of intracranial origin DENV-2 were blocked after replication in Vero cells and caused limited cell_-cell membrane fusion in Vero cells.…”