ArticleJournal of virology1999
Mutational analysis of the putative fusion domain of Ebola virus glycoprotein.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 146 citations in OpenAlex.
- Genome-wide CRISPR/Cas9 screen identifies SLC39A9 and PIK3C3 as crucial entry factors for Ebola virus infection.PLoS pathogens · 2024Article
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Pseudotyped Viruses for Marburgvirus and Ebolavirus.Advances in experimental medicine and biology · 2023Article
- Glycan shield of the ebolavirus envelope glycoprotein GP.Communications biology · 2022Article
- Vesicular Stomatitis Virus: From Agricultural Pathogen to Vaccine Vector.Pathogens (Basel, Switzerland) · 2021Review
- Animal and human RNA viruses: genetic variability and ability to overcome vaccines.Archives of microbiology · 2021Review
- Virus-Mediated Cell-Cell Fusion.International journal of molecular sciences · 2020Review
- Article
- Conformational changes in the Ebola virus membrane fusion machine induced by pH, Ca2+, and receptor binding.PLoS biology · 2020Article
- A versatile platform technology for recombinant vaccines using non-propagative human parainfluenza virus type 2 vector.Scientific reports · 2019Article
- Review of computational methods for virus-host protein interaction prediction: a case study on novel Ebola-human interactions.Briefings in functional genomics · 2018Review
- Identity and validity of conserved B cell epitopes of filovirus glycoprotein: towards rapid diagnostic testing for Ebola and possibly Marburg virus disease.BMC infectious diseases · 2018Article
- Immunogenicity of propagation-restricted vesicular stomatitis virus encoding Ebola virus glycoprotein in guinea pigs.The Journal of general virology · 2018Article
- Purification and characterization of monoclonal IgG antibodies recognizing Ebola virus glycoprotein.Clinical and experimental vaccine research · 2018Article
- Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles.PLoS pathogens · 2018Article
- Structure-Function Dissection of Pseudorabies Virus Glycoprotein B Fusion Loops.Journal of virology · 2018Article
- The lifecycle of the Ebola virus in host cells.Oncotarget · 2017Review
- Preferential production of IgM-secreting hybridomas by immunization with DNA vaccines coding for Ebola virus glycoprotein: use of protein boosting for IgG-secreting hybridoma production.Clinical and experimental vaccine research · 2017Article
- A Polymorphism within the Internal Fusion Loop of the Ebola Virus Glycoprotein Modulates Host Cell Entry.Journal of virology · 2017Article
- Biochemical Basis for Increased Activity of Ebola Glycoprotein in the 2013-16 Epidemic.Cell host & microbe · 2017Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ebola viruses contain a single glycoprotein (GP) spike, which functions as a receptor binding and membrane fusion protein. It contains a highly conserved hydrophobic region (amino acids 524 to 539) located 24 amino acids downstream of the N terminus of the Ebola virus GP2 subunit. Comparison of this region with the structural features of the transmembrane subunit of avian retroviral GPs suggests that the conserved Ebola virus hydrophobic region may, in fact, serve as the fusion peptide. To test this hypothesis directly, we introduced conservative (alanine) and nonconservative (arginine) amino acid substitutions at eight positions in this region of the GP2 molecule. The effects of these mutations were deduced from the ability of the Ebola virus GP to complement the infectivity of a vesicular stomatitis virus (VSV) lacking the receptor-binding G protein. Some mutations, such as Ile-to-Arg substitutions at positions 532 (I532R), F535R, G536A, and P537R, almost completely abolished the ability of the GP to support VSV infectivity without affecting the transport of GP to the cell surface and its incorporation into virions or the production of virus particles. Other mutations, such as G528R, L529A, L529R, I532A, and F535A, reduced the infectivity of the VSV-Ebola virus pseudotypes by at least one-half. These findings, together with previous reports of liposome association with a peptide corresponding to positions 524 to 539 in the GP molecule, offer compelling support for a fusion peptide role for the conserved hydrophobic region in the Ebola virus GP.
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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.