ReviewAdvances in experimental medicine and biology2013
Class II fusion proteins.
Review in Advances in experimental medicine and biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- Andes virus and the aging host: lessons from the 2026 outbreak and a framework for age-related disease severity.GeroScience · 2026Review
- Pathogenicity and virulence of Rodent-Borne Orthohantaviruses.Virulence · 2025Review
- Single-dose VSV-based vaccine protects against Kyasanur Forest disease in nonhuman primates.Science advances · 2023Article
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Review
- DMP8 and 9 regulate HAP2/GCS1 trafficking for the timely acquisition of sperm fusion competence.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis of synergistic neutralization of Crimean-Congo hemorrhagic fever virus by human antibodies.Science (New York, N.Y.) · 2022Article
- Genome-Wide Approaches to Unravel the Host Factors Involved in Chikungunya Virus Replication.Frontiers in microbiology · 2022Review
- Inhibition of Viral Membrane Fusion by Peptides and Approaches to Peptide Design.Pathogens (Basel, Switzerland) · 2021Review
- Review
- Species-specific gamete recognition initiates fusion-driving trimer formation by conserved fusogen HAP2.Nature communications · 2021Article
- Domains and Functions of Spike Protein in Sars-Cov-2 in the Context of Vaccine Design.Viruses · 2021Review
- Identification and Characteristics of Fusion Peptides Derived From Enveloped Viruses.Frontiers in chemistry · 2021Review
- Molecular rationale for antibody-mediated targeting of the hantavirus fusion glycoprotein.eLife · 2020Article
- Entry Inhibitors: Efficient Means to Block Viral Infection.The Journal of membrane biology · 2020Review
- Anti-Chikungunya Virus Monoclonal Antibody That Inhibits Viral Fusion and Release.Journal of virology · 2020Article
- Review
- Plant sperm need a little help.Nature plants · 2019Article
- A protein coevolution method uncovers critical features of the Hepatitis C Virus fusion mechanism.PLoS pathogens · 2018Article
- Probing the antigenicity of hepatitis C virus envelope glycoprotein complex by high-throughput mutagenesis.PLoS pathogens · 2017Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enveloped viruses rely on fusion proteins in their envelope to fuse the viral membrane to the host-cell membrane. This key step in viral entry delivers the viral genome into the cytoplasm for replication. Although class II fusion proteins are genetically and structurally unrelated to class I fusion proteins, they use the same physical principles and topology as other fusion proteins to drive membrane fusion. Exposure of a fusion loop first allows it to insert into the host-cell membrane. Conserved hydrophobic residues in the fusion loop act as an anchor, which penetrates only partway into the outer bilayer leaflet of the host-cell membrane. Subsequent folding back of the fusion protein on itself directs the C-terminal viral transmembrane anchor towards the fusion loop. This fold-back forces the host-cell membrane (held by the fusion loop) and the viral membrane (held by the C-terminal transmembrane anchor) against each other, resulting in membrane fusion. In class II fusion proteins, the fold-back is triggered by the reduced pH of an endosome, and is accompanied by the assembly of fusion protein monomers into trimers. The fold-back occurs by domain rearrangement rather than by an extensive refolding of secondary structure, but this domain rearrangement and the assembly of monomers into trimers together bury a large surface area. The energy that is thus released exerts a bending force on the apposed viral and cellular membranes, causing them to bend towards each other and, eventually, to fuse.
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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.