ArticleThe Journal of biological chemistry2012
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.
Article in The Journal of biological chemistry, 2012. 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, 42 citations in OpenAlex.
- 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
- Entry of Enveloped Viruses into Host Cells: Membrane Fusion.Sub-cellular biochemistry · 2024Review
- SARS-CoV-2 infection and viral fusogens cause neuronal and glial fusion that compromises neuronal activity.Science advances · 2023Article
- 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
- N-Myristoyltransferase as a Glycine and Lysine Myristoyltransferase in Cancer, Immunity, and Infections.ACS chemical biology · 2020Review
- 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
- Cell-cell fusion induced by reovirus FAST proteins enhances replication and pathogenicity of non-enveloped dsRNA viruses.PLoS pathogens · 2019Article
- Phage Lysis: Multiple Genes for Multiple Barriers.Advances in virus research · 2019Review
- Reovirus FAST Protein Enhances Vesicular Stomatitis Virus Oncolytic Virotherapy in Primary and Metastatic Tumor Models.Molecular therapy oncolytics · 2017Article
- Genetic Analysis of the Lambda Spanins Rz and Rz1: Identification of Functional Domains.G3 (Bethesda, Md.) · 2017Article
- Reovirus FAST Proteins Drive Pore Formation and Syncytiogenesis Using a Novel Helix-Loop-Helix Fusion-Inducing Lipid Packing Sensor.PLoS pathogens · 2015Article
- Membrane fusion during phage lysis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Kinetics of lipid mixing between bicelles and nanolipoprotein particles.Biophysical chemistry · 2015Article
- Efficient reovirus- and measles virus-mediated pore expansion during syncytium formation is dependent on annexin A1 and intracellular calcium.Journal of virology · 2014Article
- Reovirus-associated meningoencephalomyelitis in baboons.Veterinary pathology · 2014Article
- A compact, multifunctional fusion module directs cholesterol-dependent homomultimerization and syncytiogenic efficiency of reovirus p10 FAST proteins.PLoS pathogens · 2014Article
- Entry of enveloped viruses into host cells: membrane fusion.Sub-cellular biochemistry · 2013Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The p15 fusion-associated small transmembrane (FAST) protein is a nonstructural viral protein that induces cell-cell fusion and syncytium formation. The exceptionally small, myristoylated N-terminal ectodomain of p15 lacks any of the defining features of a typical viral fusion protein. NMR and CD spectroscopy indicate this small fusion module comprises a left-handed polyproline type II (PPII) helix flanked by small, unstructured N and C termini. Individual prolines in the 6-residue proline-rich motif are highly tolerant of alanine substitutions, but multiple substitutions that disrupt the PPII helix eliminate cell-cell fusion activity. A synthetic p15 ectodomain peptide induces lipid mixing between liposomes, but with unusual kinetics that involve a long lag phase before the onset of rapid lipid mixing, and the length of the lag phase correlates with the kinetics of peptide-induced liposome aggregation. Lipid mixing, liposome aggregation, and stable peptide-membrane interactions are all dependent on both the N-terminal myristate and the presence of the PPII helix. We present a model for the mechanism of action of this novel viral fusion peptide, whereby the N-terminal myristate mediates initial, reversible peptide-membrane binding that is stabilized by subsequent amino acid-membrane interactions. These interactions induce a biphasic membrane fusion reaction, with peptide-induced liposome aggregation representing a distinct, rate-limiting event that precedes membrane merger. Although the prolines in the proline-rich motif do not directly interact with membranes, the PPII helix may function to force solvent exposure of hydrophobic amino acid side chains in the regions flanking the helix to promote membrane binding, apposition, and fusion.
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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.