ArticleVirology journal2022
The role of N-linked glycosylation in proteolytic processing and cell surface transport of the Cedar virus fusion protein.
Article in Virology journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- N-glycosylation of the PEDV spike protein modulates viral replication and pathogenicity.Veterinary research · 2025Article
- Unveiling emerging threats: Langya and Mojiang-A dance with unfamiliar foes.Infectious diseases & immunity · 2025Review
- Examination of respiratory syncytial virus fusion protein proteolytic processing and roles of the P27 domain.Journal of virology · 2024Article
- Structure and antigenicity of divergent Henipavirus fusion glycoproteins.Nature communications · 2023Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundN-linked glycans on viral glycoproteins have been shown to be important for protein expression, processing and intracellular transport. The fusion glycoprotein F of Cedar virus (CedV) contains six potential N-glycosylation sites.
findingsTo investigate their impact on cell surface transport, proteolytic cleavage and biological activity, we disrupted the consensus sequences by conservative mutations (Asn to Gln) and found that five of the six potential N-glycosylation sites are actually utilized. The individual removal of N-glycan g1 (N66), g2 (N79) and g3 (N98) in the CedV F
conclusionsOur findings indicate that the individual N-linked modifications, with the exception of glycan g4, are dispensable for processing of CedV F protein in transfection experiments. However, removal of g4 led to a phenotype that was strongly impaired concerning cell surface expression and proteolytic activation.
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