ArticlePLoS pathogens2010
Steric shielding of surface epitopes and impaired immune recognition induced by the ebola virus glycoprotein.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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Who cites it
102 citing papers in PubMed, 144 citations in OpenAlex.
- Serological and transcriptomic response of African fruit bats to immune challenge with recombinant vaccines expressing Ebola or Nipah virus antigens.Royal Society open science · 2026Article
- The Biological Role of Enveloped Virus Glycosylation and Its Interactions with Antiviral Lectins.Advances in experimental medicine and biology · 2026Review
- Rational design of next-generation filovirus vaccines combining glycoprotein stabilization and nanoparticle display with glycan modification.Nature communications · 2025Article
- Immunogenicity of differentially glycosylated Marburg virus glycoproteins expressed in mammalian and insect cells.Virology journal · 2025Article
- Rational design of next-generation filovirus vaccines through glycoprotein stabilization, nanoparticle display, and glycan modification.bioRxiv : the preprint server for biology · 2025Article
- Immunological insights into the re-emergence of human metapneumovirus.Current opinion in immunology · 2025Review
- Mapping Immunological, Host Receptor Binding Determinants, and Cathepsin Cleavage Site of EBOV Glycoprotein Utilizing the Qubevirus Platform.ACS omega · 2025Article
- Article
- Glycan masking in immunogen design: computational and experimental methods.Frontiers in immunology · 2025Review
- Viral manipulation of the HLA class I antigen processing and presentation pathway.Frontiers in immunology · 2025Review
- Afucosylated anti-EBOV antibody MIL77-3 engages sGP to elicit NK cytotoxicity.Journal of virology · 2024Article
- A toxicology study ofMolecular therapy. Methods & clinical development · 2024Article
- A replicating RNA vaccine confers protection in a rhesus macaque model of Crimean-Congo hemorrhagic fever.NPJ vaccines · 2024Article
- A rabies virus-vectored vaccine expressing two copies of the Marburg virus glycoprotein gene induced neutralizing antibodies against Marburg virus in humanized mice.Emerging microbes & infections · 2023Article
- The Mucin-Like Domain of the Ebola Glycoprotein Does Not Impact Virulence or Pathogenicity in Ferrets.The Journal of infectious diseases · 2023Article
- Development of a dual vaccine against East Coast fever and lumpy skin disease.Frontiers in immunology · 2023Article
- An RSV Live-Attenuated Vaccine Candidate Lacking G Protein Mucin Domains Is Attenuated, Immunogenic, and Effective in Preventing RSV in BALB/c Mice.The Journal of infectious diseases · 2022Article
- RNF185 regulates proteostasis in Ebolavirus infection by crosstalk between the calnexin cycle, ERAD, and reticulophagy.Nature communications · 2022Article
- Article
- Antibody bivalency improves antiviral efficacy by inhibiting virion release independently of Fc gamma receptors.Cell reports · 2022Article
42 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Many viruses alter expression of proteins on the surface of infected cells including molecules important for immune recognition, such as the major histocompatibility complex (MHC) class I and II molecules. Virus-induced downregulation of surface proteins has been observed to occur by a variety of mechanisms including impaired transcription, blocks to synthesis, and increased turnover. Viral infection or transient expression of the Ebola virus (EBOV) glycoprotein (GP) was previously shown to result in loss of staining of various host cell surface proteins including MHC1 and β1 integrin; however, the mechanism responsible for this effect has not been delineated. In the present study we demonstrate that EBOV GP does not decrease surface levels of β1 integrin or MHC1, but rather impedes recognition by steric occlusion of these proteins on the cell surface. Furthermore, steric occlusion also occurs for epitopes on the EBOV glycoprotein itself. The occluded epitopes in host proteins and EBOV GP can be revealed by removal of the surface subunit of GP or by removal of surface N- and O- linked glycans, resulting in increased surface staining by flow cytometry. Importantly, expression of EBOV GP impairs CD8 T-cell recognition of MHC1 on antigen presenting cells. Glycan-mediated steric shielding of host cell surface proteins by EBOV GP represents a novel mechanism for a virus to affect host cell function, thereby escaping immune detection.
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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.