N-glycosylation, a leading role in viral infection and immunity development

Abstract

N- linked protein glycosylation is an essential co-and posttranslational protein modification that occurs in all three domains of life; the assembly of N- glycans follows a complex sequence of events spanning the (Endoplasmic Reticulum) ER and the Golgi apparatus. It has a significant impact on both physicochemical properties and biological functions. It plays a significant role in protein folding and quality control, glycoprotein interaction, signal transduction, viral attachment, and immune response to infection. Glycoengineering of protein employed for improving protein properties and plays a vital role in the production of recombinant glycoproteins and struggles to humanize recombinant therapeutic proteins. It considers an alternative platform for biopharmaceuticals production. Many immune proteins and antibodies are glycosylated. Pathogen’s glycoproteins play vital roles during the infection cycle and their expression of specific oligosaccharides via the N -glycosylation pathway to evade detection by the host immune system. This review focuses on the aspects of N -glycosylation processing, glycoengineering approaches, their role in viral attachment, and immune responses to infection. Supplementary Information The online version contains supplementary material available at 10.1007/s11033-022-07359-4.

Spike protein receptor-binding domains from SARS-CoV-2 variants of interest bind human ACE2 more tightly than the prototype spike protein

“…Glycosylation is a post-translational modification that can have important implications for the cell. N-linked glycosylation contributes to protein folding, quality control, signal transduction, and viral attachment [ 20 ]. Glycosylation of the HIV virus assists in the evasion of the immune response via shielding of immunogenic epitopes [ 21 ].…”

Insect cell‐derived human CD200‐Fc increases zonula occludens‐1 tight junction protein in urothelial carcinoma cells

“…The glycosylation of proteins has important functional effects on protein activity, half-life, biological recognition of the epitope and antigenicity (Lee et al 2015). In addition, it plays an important role in the folding of peptide chains, solubility and resistance to proteolysis during protein production (Pandey et al 2022). The binding interaction between CD200-Fc I and anti-CD200 antibody was verified using ELISA.…”

“…In addition, it plays an important role in the folding of peptide chains, solubility and resistance to proteolysis during protein production (Pandey et al . 2022). The binding interaction between CD200‐Fc I and anti‐CD200 antibody was verified using ELISA.…”

Importance of N-Glycosylation for the Expression and Function of Human Organic Anion Transporting Polypeptide 2B1

“…19 It can be mainly classified into six categories: N-glycosylation, O-glycosylation, C-glycosylation, S-glycosylation, P-glycosylation, and glypiation (GPI-anchored). 20,21 More than 50% of the mammalian proteome and nearly all SLC transporters are glycosylated, with Nglycosylation being the most common type. 22,23 N-linked glycosylation is the process of enzymatic addition of oligosaccharides to extracellular asparagine residues, predominantly at the N-X-T/S motif, where X is any amino acid except proline.…”

“…It was estimated that there are more than 400 different types of post-translational modifications. , Among them, protein glycosylation is considered as one of the major post-translational modifications, which has significant effects on protein folding, conformation, trafficking, stability, and activity . It can be mainly classified into six categories: N-glycosylation, O-glycosylation, C-glycosylation, S-glycosylation, P-glycosylation, and glypiation (GPI-anchored). , More than 50% of the mammalian proteome and nearly all SLC transporters are glycosylated, with N-glycosylation being the most common type. , …”