ArticleThe Journal of biological chemistry2010
Features of a spatially constrained cystine loop in the p10 FAST protein ectodomain define a new class of viral fusion peptides.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Multiple rotavirus species encode fusion-associated small transmembrane (FAST) proteins with cell type-specific activity.Journal of virology · 2025Article
- Avian deltacoronaviruses encode fusion-associated small transmembrane proteins that can induce syncytia formation.Virology · 2024Article
- Nonstructural protein NS17 of grass carp reovirus Honghu strain promotes virus infection by mediating cell-cell fusion and apoptosis.Virus research · 2023Article
- Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide.The Journal of membrane biology · 2022Review
- Review
- Evolutionarily related small viral fusogens hijack distinct but modular actin nucleation pathways to drive cell-cell fusion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Polycistronic Genome Segment Evolution and Gain and Loss of FAST Protein Function during Fusogenic Orthoreovirus Speciation.Viruses · 2020Article
- Cell Fusion: Merging Membranes and Making Muscle.Trends in cell biology · 2019Review
- Rotavirus Species B Encodes a Functional Fusion-Associated Small Transmembrane Protein.Journal of virology · 2019Article
- Cell-cell fusion induced by reovirus FAST proteins enhances replication and pathogenicity of non-enveloped dsRNA viruses.PLoS pathogens · 2019Article
- A Bat-Derived Putative Cross-Family Recombinant Coronavirus with a Reovirus Gene.PLoS pathogens · 2016Article
- Article
- Reovirus FAST Proteins Drive Pore Formation and Syncytiogenesis Using a Novel Helix-Loop-Helix Fusion-Inducing Lipid Packing Sensor.PLoS pathogens · 2015Article
- Efficient reovirus- and measles virus-mediated pore expansion during syncytium formation is dependent on annexin A1 and intracellular calcium.Journal of virology · 2014Article
- Golgi complex-plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal.Molecular biology of the cell · 2014Article
- A compact, multifunctional fusion module directs cholesterol-dependent homomultimerization and syncytiogenic efficiency of reovirus p10 FAST proteins.PLoS pathogens · 2014Article
- Cell-cell membrane fusion induced by p15 fusion-associated small transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix.The Journal of biological chemistry · 2012Article
- Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Helix-destabilizing, beta-branched, and polar residues in the baboon reovirus p15 transmembrane domain influence the modularity of FAST proteins.Journal of virology · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The reovirus fusion-associated small transmembrane (FAST) proteins are the smallest known viral membrane fusion proteins. With ectodomains of only approximately 20-40 residues, it is unclear how such diminutive fusion proteins can mediate cell-cell fusion and syncytium formation. Contained within the 40-residue ectodomain of the p10 FAST protein resides an 11-residue sequence of moderately apolar residues, termed the hydrophobic patch (HP). Previous studies indicate the p10 HP shares operational features with the fusion peptide motifs found within the enveloped virus membrane fusion proteins. Using biotinylation assays, we now report that two highly conserved cysteine residues flanking the p10 HP form an essential intramolecular disulfide bond to create a cystine loop. Mutagenic analyses revealed that both formation of the cystine loop and p10 membrane fusion activity are highly sensitive to changes in the size and spatial arrangement of amino acids within the loop. The p10 cystine loop may therefore function as a cystine noose, where fusion peptide activity is dependent on structural constraints within the noose that force solvent exposure of key hydrophobic residues. Moreover, inhibitors of cell surface thioreductase activity indicate that disruption of the disulfide bridge is important for p10-mediated membrane fusion. This is the first example of a viral fusion peptide composed of a small, spatially constrained cystine loop whose function is dependent on altered loop formation, and it suggests the p10 cystine loop represents a new class of viral fusion peptides.
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