ArticleBiochemistry2007
A conserved region between the heptad repeats of paramyxovirus fusion proteins is critical for proper F protein folding.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Adaptor complex-mediated trafficking of Newcastle disease virus fusion protein is regulated by the YLMY motif of its cytoplasmic tail.Virulence · 2022Article
- Antivirals targeting paramyxovirus membrane fusion.Current opinion in virology · 2021Review
- The effect of the HRB linker of Newcastle disease virus fusion protein on the fusogenic activity.Journal of microbiology (Seoul, Korea) · 2021Article
- Third Helical Domain of the Nipah Virus Fusion Glycoprotein Modulates both Early and Late Steps in the Membrane Fusion Cascade.Journal of virology · 2020Article
- The DI-DII linker of human parainfluenza virus type 3 fusion protein is critical for the virus.Virus genes · 2020Article
- Molecular Evolution of the Fusion Protein (Frontiers in microbiology · 2019Article
- Article
- Novel Atlantic bottlenose dolphin parainfluenza virus TtPIV-1 clusters with bovine PIV-3 genotype B strains.Virus genes · 2015Article
- Trimeric transmembrane domain interactions in paramyxovirus fusion proteins: roles in protein folding, stability, and function.The Journal of biological chemistry · 2013Article
- Mutating conserved cysteines in the alphavirus e2 glycoprotein causes virus-specific assembly defects.Journal of virology · 2012Article
- Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recycling.Journal of virology · 2012Article
- A functional henipavirus envelope glycoprotein pseudotyped lentivirus assay system.Virology journal · 2010Article
- Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F protein.Journal of virology · 2010Article
- Residues in the heptad repeat a region of the fusion protein modulate the virulence of Sendai virus in mice.Journal of virology · 2010Article
- Differential rates of protein folding and cellular trafficking for the Hendra virus F and G proteins: implications for F-G complex formation.Journal of virology · 2009Article
- Signal peptide and helical bundle domains of virulent canine distemper virus fusion protein restrict fusogenicity.Journal of virology · 2007Article
- A conserved region in the F(2) subunit of paramyxovirus fusion proteins is involved in fusion regulation.Journal of virology · 2007Article
- Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Paramyxoviruses are a diverse family that utilizes a fusion (F) protein to enter cells via fusion of the viral lipid bilayer with a target cell membrane. Although certain regions of the F protein are known to play critical roles in membrane fusion, the function of much of the protein remains unclear. Sequence alignment of a set of paramyxovirus F proteins and analysis utilizing Block Maker identified a region of conserved amino acid sequence in a large domain between the heptad repeats of F1, designated CBF1. We employed site-directed mutagenesis to analyze the function of completely conserved residues of CBF1 in both the simian virus 5 (SV5) and Hendra virus F proteins. The majority of CBF1 point mutants were deficient in homotrimer formation, proteolytic processing, and transport to the cell surface. For some SV5 F mutants, proteolytic cleavage and surface expression could be restored by expression at 30 degrees C, and varying levels of fusion promotion were observed at this temperature. In addition, the mutant SV5 F V402A displayed a hyperfusogenic phenotype at both 30 and 37 degrees C, indicating that this mutation allows for efficient fusion with only an extremely small amount of cleaved, active protein. The recently published prefusogenic structure of PIV5/SV5 F (Yin, H. S., et al. (2006) Nature 439, 38-44) indicates that residues within and flanking CBF1 interact with the fusion peptide domain. Together, these data suggest that CBF1-fusion peptide interactions are critical for the initial folding of paramyxovirus F proteins from this important viral family and can also modulate subsequent membrane fusion promotion.
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