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

Figures & data

Table 1. Current understanding of glycosylation of viral proteins

Virus	Viral Protein	Glycosylation site	Potential function	References
DENV	Envelope	Asn-67	Transmission, Replication, Virus entry	[11,22]
		Asn-153	Survival in mosquito	[11,21,22]
	NS1	Asn-130	Virus growth, NS1 secretion, Cytopathy and neurovirulence	[21,144–147]
		Asn-207	Destroy endothelial layer and internalization	[21,142,143]
ZIKV	Envelope	Asn-154	Replication, Assembly, Infectivity, Neurovirulence, Apoptosis, Invasion in mosquito	[28–31]
	prM	Asn-69	Virus production, Expression and secretion of ZIKV E	[12]
	NS1	Asn-130 and Asn-207	Internalization and endothelium barrier function	[12]
WNV	Envelope	Asn-154	Assembly and infectivity of particle, Replication and infection in mosquito, Neuroinvasiveness in mice	[6,36–39]
	prM	Asn-15	Assembly and release of particle	[6]
	NS1	Asn-130, Asn-175 and Asn-207	Internalization and neuroinvasiveness in mice	[150]
JEV	Envelope	Asn-154	Replication, Neurovirulence and neuroinvasiveness in mice	[40,41]
	prM	Asn-15	prM protein Biogenesis, Virus particle release, Pathogenicity in mice	[5]
HCV	E1 and E2		Protein folding, Virus entry, Immune response, Assembly and/or secretion of viral particle	[42–45]
HIV	Env/gp120	Asn-260	Expression of gp120 and gp41, Infectivity and virus entry	[4,52–54]
IAV	HA and NA		Protein folding, transport and pH stability; Affinity of SA receptor and viral pathogenicity; Functional NA and neurovirulence in mice; Receptor binding, Infectivity, Virus release, and neurotoxicity	[56–67]
SARS-CoV-2	Spike	Asn-90 or Asn-322	Virus entry	[10,71]
EBOV	GP1		Transduction of viral particle, Sensitivity to Cathepsin B	[13,79]
	GP2	Asn-563 and Asn-618	Virus entry	[79]
SFTSV	Gn	Asn-33 and Asn-63	Immune response	[80,81]
	Gc	Asn-853, Asn-914 and Asn-936	Immune response and membrane fusion	[80,82]
HTNV	Gn	Asn-134, Asn-235, Asn-347, Asn-399 and Asn-609	Folding, Intracellular transport and epitope conformation; Maintenance of HTNV glycoprotein; Immunoreactivity	[85,86]
	Gc	Asn-928	Immunoreactivity	[86]
RVF	Gn	Asn-438	Infection and inducing neutralizing antibodies	[87–89]
	Gc	Asn-794, Asn-829, Asn-1035, and Asn-1077	Infection and inducing neutralizing antibodies	[87–89]
NiV	F and G		Virus entry, Antibody neutralization and cell-cell fusion	[92,93]
HeV	F and G		Virus attachment and membrane fusion	[94]
HRSV	F	Asn-27, Asn-70, Asn-116, Asn-126 and Asn-500	Attachment, Replication and Infection; Syncytium formation and antigenicity of F protein	[95–97]
	G		Membrane fusion	[95]
LCMV	GP1	Asn-87, Asn-97, and Asn-104	Folding of GPC and virus adaptability	[8,99,100]
	GP2	Asn-234 or Asn-379/381	Membrane fusion and virus adaptability	[8,100]
LASV	GP1/GP2	Asn-89, Asn-99, Asn-109, Asn-119, Asn-167, Asn-365 and Asn-373	Envelope glycoprotein cleavage, Infectivity and immune response	[9,102–107]
HBV	S	Asn-146	Production of infectious virus particles	[108]
HSV-1	gB, gC, gD, gE gH/gL, gK, gI		Attachment, Penetration, Membrane fusion, Receptor interactions; Immunity interference, Pathogenesis, Production of noninfectious virus particles, Infectivity	[111,113–119,126–128]
VZV	gB, gC, gE, gH, gI, gK, and gL		Assembly,Trafficking, Reproduction, Replication, virion-cell, cell-cell fusion, Cell-to-cell spread and infectivity	[129–133]

Figure 1. Diverse functions of glycosylation of viral proteins from mosquito-borne flaviviruses.

Note: The structural proteins (E and prM) and nonstructural protein NS1 of flaviviruses are glycosylated and play multiple roles in the entire lifecycle of viruses. 1) Glycosylations of viral proteins influence virus binding and evasion. 2) Glycosylation of viral protein affects viral lifecycle in cells, including replication, translation, assembly, and release. 3) Glycosylations of viral proteins play a role in viral survival and transmission in mosquitoes. 4) Glycosylation of viral proteins determines viruses’ pathogenicity in mammalian hosts. The 3-D models used for representing the flavivirus protein structures were cited from the PDB database (PDB accession numbers: ITG8, 4OIG, 2HG0, 4O6C, 5MV1, 5O36, 5JHM, 3C5X, and 5K6K). The glycan chains represented here are hypothetical schematic sketches.

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Data availability statement

Data sharing not applicable to this article as no data sets were generated or analyzed during the current study. Data cited in this review are published and available online or upon request from the authors of the respective publications.