ArticleJournal of virology2005
Unusual topological arrangement of structural motifs in the baboon reovirus fusion-associated small transmembrane protein.
Article in Journal of virology, 2005. 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, 53 citations in OpenAlex.
- Review
- 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
- Fusogenic vesicular stomatitis virus combined with natural killer T cell immunotherapy controls metastatic breast cancer.Breast cancer research : BCR · 2024Article
- Virus-Induced Cell Fusion and Syncytia Formation.Results and problems in cell differentiation · 2024Article
- Nonstructural protein NS17 of grass carp reovirus Honghu strain promotes virus infection by mediating cell-cell fusion and apoptosis.Virus research · 2023Article
- The nonstructural p17 protein of a fusogenic bat-borne reovirus regulates viral replication in virus species- and host-specific manners.PLoS pathogens · 2022Article
- Review
- Polycistronic Genome Segment Evolution and Gain and Loss of FAST Protein Function during Fusogenic Orthoreovirus Speciation.Viruses · 2020Article
- 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
- Reovirus FAST Protein Enhances Vesicular Stomatitis Virus Oncolytic Virotherapy in Primary and Metastatic Tumor Models.Molecular therapy oncolytics · 2017Article
- 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
- Lysophosphatidylcholine reversibly arrests pore expansion during syncytium formation mediated by diverse viral fusogens.Journal of virology · 2014Article
- Reovirus-associated meningoencephalomyelitis in baboons.Veterinary pathology · 2014Article
- Golgi complex-plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal.Molecular biology of the cell · 2014Article
- Polybasic trafficking signal mediates golgi export, ER retention or ER export and retrieval based on membrane-proximity.PloS one · 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
- 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
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Select members of the Reoviridae are the only nonenveloped viruses known to induce syncytium formation. The fusogenic orthoreoviruses accomplish cell-cell fusion through a distinct class of membrane fusion-inducing proteins referred to as the fusion-associated small transmembrane (FAST) proteins. The p15 membrane fusion protein of baboon reovirus is unique among the FAST proteins in that it contains two hydrophobic regions (H1 and H2) recognized as potential transmembrane (TM) domains, suggesting a polytopic topology. However, detailed topological analysis of p15 indicated only the H1 domain is membrane spanning. In the absence of an N-terminal signal peptide, the H1 TM domain serves as a reverse signal-anchor to direct p15 membrane insertion and a bitopic N(exoplasmic)/C(cytoplasmic) topology. This topology results in the translocation of the smallest ectodomain ( approximately 20 residues) of any known viral fusion protein, with the majority of p15 positioned on the cytosolic side of the membrane. Mutagenic analysis indicated the unusual presence of an N-terminal myristic acid on the small p15 ectodomain is essential to the fusion process. Furthermore, the only other hydrophobic region (H2) present in p15, aside from the TM domain, is located within the endodomain. Consequently, the p15 ectodomain is devoid of a fusion peptide motif, a hallmark feature of membrane fusion proteins. The exceedingly small, myristoylated ectodomain and the unusual topological distribution of structural motifs in this nonenveloped virus membrane fusion protein necessitate alternate models of protein-mediated membrane fusion.
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