Establishment of a system to quantify wild‐type herpes simplex virus–induced cell–cell fusion reveals a role of N‐glycosylation of HSV‐1 envelope glycoprotein B in cell–cell fusion

Fukui, Ayano; Maruzuru, Yuhei; Takeshima, Koki; Koyanagi, Naoto; Kawaguchi, Yasushi

doi:10.1111/1348-0421.13050

Cited by 3 publications

(1 citation statement)

References 18 publications

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“…Typically, viruses contribute to their virulence by manipulating or evading the host's immune response capabilities [28,29]. Herpesvirus glycoproteins gB, gH, gD, gJ, and gM are all connected via asparagine-linked glycosylation, which plays an essential role in their proper folding, transport, and immune evasion [9,[30][31][32][33][34]. However, the precise role of DPV gI glycosylation in the context of viral proliferation and virulence within its natural host is an area that requires further investigation.…”

Section: Introductionmentioning

confidence: 99%

N-glycosylation of envelope glycoprotein gI is crucial for the duck plague virus proliferation and virulence

Cheng,

Ning,

Wang

et al. 2024

Preprint

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Duck plague virus (DPV) causes highly pathogenic duck plague, and the envelope glycoprotein gI, as one of the key virulence genes, has not yet had its critical virulence sites identified through screening. In this study, reverse genetics technology was utilized to specifically target the gI protein within the genome of the DPV. Four mutant strains of DPV with mutations in the N-glycosylation sites of the gI protein were designed and constructed, and these mutant strains were successfully rescued. Our results confirmed that three asparagine residues (N69, N78, and N265) of gI are N-glycosylation sites, and Western blot analysis substantiated that the glycosylation at each predicted N-glycosylation site was compromised. The deglycosylation of gI results in the misfolding of the protein and its consequent retention in the endoplasmic reticulum (ER). For the subsequent intracellular transport of gI within duck embryonic fibroblasts (DEFs), the carrying effect of its interacting protein gE is essential. Compared to the parental virus, the mutated virus exhibits a reduced intercellular transmission capability to 66.3%. In ducks, the deglycosylation of gI significantly reduces the replication of DPV in vivo, thereby impairing the virulence of DPV. This research marks the first successful generation of an attenuated DPV strain through targeted mutations at the N-glycosylation sites. The findings provide a foundational understanding of DPV pathogenesis and offer a basis for the development of live attenuated vaccines against the disease.

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Section: Introductionmentioning

confidence: 99%

N-glycosylation of envelope glycoprotein gI is crucial for the duck plague virus proliferation and virulence

Cheng,

Ning,

Wang

et al. 2024

Preprint

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Interaction of the Hemagglutinin Stalk Region with Cell Adhesion Molecule (CADM) 1 and CADM2 Mediates the Spread between Neurons and Neuropathogenicity of Measles Virus with a Hyperfusogenic Fusion Protein

Takemoto

Hirai

Watanabe

et al. 2023

J Virol

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The Effects of Herpes Virus Glycoprotein Glycosylation On Viral Infection and Pathogenesis

Chen,

Liu,

Luo

2023

Future Virol.

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Herpes virus is an enveloped virus with many glycoproteins essential for viral infection and immune evasion. Several glycosylation sites exist on the glycoproteins of herpes viruses, including N- and O-glycosylation sites. Glycosylation affects herpes virus infection and pathogenesis in different ways, including the attachment and entry of the herpes virus into host cells, virus replication and the host's immune function. This article summarized the current knowledge on the glycosylation of herpes virus envelope glycoproteins and its impact on viral infection and demonstrated several applications of glycosylation inhibitors.

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Establishment of a system to quantify wild‐type herpes simplex virus–induced cell–cell fusion reveals a role of N‐glycosylation of HSV‐1 envelope glycoprotein B in cell–cell fusion

Cited by 3 publications

References 18 publications

N-glycosylation of envelope glycoprotein gI is crucial for the duck plague virus proliferation and virulence

N-glycosylation of envelope glycoprotein gI is crucial for the duck plague virus proliferation and virulence

Interaction of the Hemagglutinin Stalk Region with Cell Adhesion Molecule (CADM) 1 and CADM2 Mediates the Spread between Neurons and Neuropathogenicity of Measles Virus with a Hyperfusogenic Fusion Protein

The Effects of Herpes Virus Glycoprotein Glycosylation On Viral Infection and Pathogenesis

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