ReviewViruses2021
The Viral Class II Membrane Fusion Machinery: Divergent Evolution from an Ancestral Heterodimer.
Review in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Molecular determinants of species-specific gamete adhesion triggering HAP2-mediated membrane fusion.Nature communications · 2026Article
- Article
- GP38 is a structural component of Crimean-Congo hemorrhagic fever virus particles.Virologica Sinica · 2026Article
- Article
- The La Crosse virus Gc head domain is a major determinant of infection and pathogenesis.Journal of virology · 2025Article
- Article
- Engineering and structures of Crimean-Congo hemorrhagic fever virus glycoprotein complexes.Cell · 2025Article
- The PACS-2 protein and trafficking motifs in CCHFV Gn and Gc cytoplasmic domains govern CCHFV assembly.Emerging microbes & infections · 2024Article
- Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses.Science advances · 2024Article
- Visualizing intermediate stages of viral membrane fusion by cryo-electron tomography.Trends in biochemical sciences · 2024Review
- Article
- Molecular insight into the neutralization mechanism of human-origin monoclonal antibody AH100 against Hantaan virus.Journal of virology · 2024Article
- A ~40-kb flavi-like virus does not encode a known error-correcting mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Crimean-Congo hemorrhagic fever survivors elicit protective non-neutralizing antibodies that target 11 overlapping regions on glycoprotein GP38.Cell reports · 2024Article
- Novel requirements for HAP2/GCS1-mediated gamete fusion iniScience · 2024Article
- Engineering, structure, and immunogenicity of a Crimean-Congo hemorrhagic fever virus pre-fusion heterotrimeric glycoprotein complex.bioRxiv : the preprint server for biology · 2024Article
- Crimean-Congo Hemorrhagic Fever Survivors Elicit Protective Non-Neutralizing Antibodies that Target 11 Overlapping Regions on Viral Glycoprotein GP38.bioRxiv : the preprint server for biology · 2024Article
- Expression and Purification of RVFV Glycoprotein C for Structural Studies Using Baculovirus Expression System.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Entry of Enveloped Viruses into Host Cells: Membrane Fusion.Sub-cellular biochemistry · 2024Review
- Structural and functional analyses of viral H2 protein of the vaccinia virus entry fusion complex.Journal of virology · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A key step during the entry of enveloped viruses into cells is the merger of viral and cell lipid bilayers. This process is driven by a dedicated membrane fusion protein (MFP) present at the virion surface, which undergoes a membrane-fusogenic conformational change triggered by interactions with the target cell. Viral MFPs have been extensively studied structurally, and are divided into three classes depending on their three-dimensional fold. Because MFPs of the same class are found in otherwise unrelated viruses, their intra-class structural homology indicates horizontal gene exchange. We focus this review on the class II fusion machinery, which is composed of two glycoproteins that associate as heterodimers. They fold together in the ER of infected cells such that the MFP adopts a conformation primed to react to specific clues only upon contact with a target cell, avoiding premature fusion in the producer cell. We show that, despite having diverged in their 3D fold during evolution much more than the actual MFP, the class II accompanying proteins (AP) also derive from a distant common ancestor, displaying an invariant core formed by a β-ribbon and a C-terminal immunoglobulin-like domain playing different functional roles-heterotypic interactions with the MFP, and homotypic AP/AP contacts to form spikes, respectively. Our analysis shows that class II APs are easily identifiable with modern structural prediction algorithms, providing useful information in devising immunogens for vaccine design.
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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.