ArticleJournal of virology2003
Mutations in the cytoplasmic domain of a paramyxovirus fusion glycoprotein rescue syncytium formation and eliminate the hemagglutinin-neuraminidase protein requirement for membrane fusion.
Article in Journal of virology, 2003. 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, 43 citations in OpenAlex.
- A surface pocket in the cytoplasmic domain of the herpes simplex virus fusogen gB controls membrane fusion.PLoS pathogens · 2022Article
- Paramyxovirus Glycoproteins and the Membrane Fusion Process.Current clinical microbiology reports · 2016Article
- Unity in diversity: shared mechanism of entry among paramyxoviruses.Progress in molecular biology and translational science · 2015Review
- Mutations in the cytoplasmic domain of the Newcastle disease virus fusion protein confer hyperfusogenic phenotypes modulating viral replication and pathogenicity.Journal of virology · 2013Article
- Full conversion of the hemagglutinin-neuraminidase specificity of the parainfluenza virus 5 fusion protein by replacement of 21 amino acids in its head region with those of the simian virus 41 fusion protein.Journal of virology · 2013Article
- Nipah virus envelope-pseudotyped lentiviruses efficiently target ephrinB2-positive stem cell populations in vitro and bypass the liver sink when administered in vivo.Journal of virology · 2013Article
- Review
- Effects of stabilization of the gp41 cytoplasmic domain on fusion activity and infectivity of SIVmac239.AIDS research and human retroviruses · 2011Article
- Identification of domains on the fusion (F) protein trimer that influence the hemagglutinin-neuraminidase specificity of the f protein in mediating cell-cell fusion.Journal of virology · 2011Article
- C-terminal tyrosine residues modulate the fusion activity of the Hendra virus fusion protein.Biochemistry · 2011Article
- Viral entry mechanisms: the increasing diversity of paramyxovirus entry.The FEBS journal · 2009Review
- Multifaceted sequence-dependent and -independent roles for reovirus FAST protein cytoplasmic tails in fusion pore formation and syncytiogenesis.Journal of virology · 2009Article
- Glycoprotein interactions in paramyxovirus fusion.Future virology · 2009Article
- Enhanced fusion pore expansion mediated by the trans-acting Endodomain of the reovirus FAST proteins.PLoS pathogens · 2009Article
- Signal peptide and helical bundle domains of virulent canine distemper virus fusion protein restrict fusogenicity.Journal of virology · 2007Article
- Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling.Journal of virology · 2007Article
- Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion.Virology · 2007Article
- Fusogenic variants of a noncytopathic paramyxovirus.Journal of virology · 2007Article
- Analysis of the pH requirement for membrane fusion of different isolates of the paramyxovirus parainfluenza virus 5.Journal of virology · 2006Article
- Two domains that control prefusion stability and transport competence of the measles virus fusion protein.Journal of virology · 2006Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
SER virus is closely related to the paramyxovirus simian virus 5 (SV5) but is defective in syncytium formation. The SER virus F protein has a long cytoplasmic tail (CT) domain that has been shown to inhibit membrane fusion, and this inhibitory effect could be eliminated by truncation of the C-terminal sequence (S. Tong, M. Li, A. Vincent, R. W. Compans, E. Fritsch, R. Beier, C. Klenk, M. Ohuchi, and H.-D. Klenk, Virology 301:322-333, 2002). To study the sequence requirements for regulation of fusion, codons for SER virus F protein residues spanning amino acids 535 to 542 and 548 were mutated singly to alanines, and the two leucine residues at positions 539 and 548 were mutated doubly to alanines. We found that leu-539 and leu-548 in the CT domain played a critical role in the inhibition of fusion, as mutation of the two leucines singly to alanines partially rescued fusion, and the double mutation L539, 548A completely rescued syncytium formation. Mutation of charged residues to alanines had little effect on the suppression of fusion activity, whereas the mutation of serine residues to alanines enhanced fusion activity significantly. The L539, 548A mutant also showed extensive syncytium formation when expressed without the SER virus HN protein. By constructing a chimeric SV5-SER virus F CT protein, we also found that the inhibitory effect of the long CT of the SER virus F protein could be partially transferred to the SV5 F protein. These results demonstrate that an elongated CT of a paramyxovirus F protein interferes with membrane fusion in a sequence-dependent manner.
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