ArticleThe Journal of infectious diseases2015
The Role of Conserved N-Linked Glycans on Ebola Virus Glycoprotein 2.
Article in The Journal of infectious diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Pan-Ebolavirus nanoparticle vaccine provides protection in rodents from lethal infection by Zaire and Sudan viruses.Nature communications · 2026Article
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- N-glycosylation of the PEDV spike protein modulates viral replication and pathogenicity.Veterinary research · 2025Article
- Antibodies targeting the glycan cap of Ebola virus glycoprotein are potent inducers of the complement systemCommunications biology · 2024Article
- Modification of N-Linked Glycan Sites in Viral Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Ebola Virus Activates IRE1α-DependentViruses · 2022Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- Glycan shield of the ebolavirus envelope glycoprotein GP.Communications biology · 2022Article
- Animal and human RNA viruses: genetic variability and ability to overcome vaccines.Archives of microbiology · 2021Review
- Functional Role of N-Linked Glycosylation in Pseudorabies Virus Glycoprotein gH.Journal of virology · 2018Article
- Enhancing the antiviral potency of ER α-glucosidase inhibitor IHVR-19029 against hemorrhagic fever viruses in vitro and in vivo.Antiviral research · 2018Article
- Production and Purification of Filovirus Glycoproteins in Insect and Mammalian Cell Lines.Scientific reports · 2017Article
- Vesicular Stomatitis Virus Pseudotyped with Ebola Virus Glycoprotein Serves as a Protective, Noninfectious Vaccine against Ebola Virus Challenge in Mice.Journal of virology · 2017Article
- Mechanistic understanding ofThe Journal of biological chemistry · 2017Article
- Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
backgroundN-linked glycosylation is a common posttranslational modification found on viral glycoproteins (GPs) and involved in promoting expression, cellular attachment, protection from proteases, and antibody evasion. The GP subunit GP2 of filoviruses contains 2 completely conserved N-linked glycosylation sites (NGSs) at N563 and N618, suggesting that they have been maintained through selective pressures.
methodsWe assessed mutants lacking these glycans for expression and function to understand the role of these sites during Ebola virus entry.
resultsElimination of either GP2 glycan individually had a modest effect on GP expression and no impact on antibody neutralization of vesicular stomatitis virus pseudotyped with Ebola virus GP. However, loss of the N563 glycan enhanced entry by 2-fold and eliminated GP detection by a well-characterized monoclonal antibody KZ52. Loss of both sites dramatically decreased GP expression and abolished entry. Surprisingly, a GP that retained a single NGS at N563, eliminating the remaining 16 NGSs from GP1 and GP2, had detectable expression, a modest increase in entry, and pronounced sensitivity to antibody neutralization.
conclusionsOur findings support the importance of the GP2 glycans in GP expression/structure, transduction efficiency, and antibody neutralization, particularly when N-linked glycans are also removed from GP1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.