ArticleJournal of virology2013
Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 56 citations in OpenAlex.
- Mumps Virus: Replication, Immune Response, and the Changing Landscape of Vaccine Effectiveness.Pathogens (Basel, Switzerland) · 2026Review
- Structural basis for potent neutralization of human respirovirus type 3 by protective single-domain camelid antibodies.Nature communications · 2024Article
- Structural Studies of Henipavirus Glycoproteins.Viruses · 2024Review
- A Receptor Integrin β1 Promotes Infection of Avian Metapneumovirus Subgroup C by Recognizing a Viral Fusion Protein RSD Motif.International journal of molecular sciences · 2024Article
- Structures of Langya Virus Fusion Protein Ectodomain in Pre- and Postfusion Conformation.Journal of virology · 2023Article
- PCR-Based Detection and Genetic Characterization of Parainfluenza Virus 5 Detected in Pigs in Korea from 2016 to 2018.Veterinary sciences · 2023Article
- YLMY Tyrosine Residue within the Cytoplasmic Tail of Newcastle Disease Virus Fusion Protein Regulates Its Surface Expression to Modulate Viral Budding and Pathogenicity.Microbiology spectrum · 2021Article
- The effect of the HRB linker of Newcastle disease virus fusion protein on the fusogenic activity.Journal of microbiology (Seoul, Korea) · 2021Article
- Molecular detection and whole genome characterization of Canine Parainfluenza type 5 in Thailand.Scientific reports · 2021Article
- EphrinB2 clustering by Nipah virus G is required to activate and trap F intermediates at supported lipid bilayer-cell interfaces.Science advances · 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
- Parainfluenza virus 5 fusion protein maintains pre-fusion stability but not fusogenic activity following mutation of a transmembrane leucine/isoleucine domain.The Journal of general virology · 2020Article
- Receptor-mediated cell entry of paramyxoviruses: Mechanisms, and consequences for tropism and pathogenesis.The Journal of biological chemistry · 2020Review
- The DI-DII linker of human parainfluenza virus type 3 fusion protein is critical for the virus.Virus genes · 2020Article
- Differential Features of Fusion Activation within theViruses · 2020Review
- NovelViruses · 2019Article
- Genotype replacement of the human parainfluenza virus type 2 in Croatia between 2011 and 2017 - the role of neutralising antibodies.Epidemiology and infection · 2018Article
- Functional analysis of amino acids at stalk/head interface of human parainfluenza virus type 3 hemagglutinin-neuraminidase protein in the membrane fusion process.Virus genes · 2018Article
- The Hemagglutinin-Neuraminidase (HN) Head Domain and the Fusion (F) Protein Stalk Domain of the Parainfluenza Viruses Affect the Specificity of the HN-F Interaction.Frontiers in microbiology · 2018Article
- Multiple Strategies Reveal a Bidentate Interaction between the Nipah Virus Attachment and Fusion Glycoproteins.Journal of virology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Paramyxovirus membrane glycoproteins F (fusion protein) and HN, H, or G (attachment protein) are critical for virus entry, which occurs through fusion of viral and cellular envelopes. The F protein folds into a homotrimeric, metastable prefusion form that can be triggered by the attachment protein to undergo a series of structural rearrangements, ultimately folding into a stable postfusion form. In paramyxovirus-infected cells, the F protein is activated in the Golgi apparatus by cleavage adjacent to a hydrophobic fusion peptide that inserts into the target membrane, eventually bringing the membranes together by F refolding. However, it is not clear how the attachment protein, known as HN in parainfluenza virus 5 (PIV5), interacts with F and triggers F to initiate fusion. To understand the roles of various F protein domains in fusion triggering and metastability, single point mutations were introduced into the PIV5 F protein. By extensive study of F protein cleavage activation, surface expression, and energetics of fusion triggering, we found a role for an immunoglobulin-like (Ig-like) domain, where multiple hydrophobic residues on the PIV5 F protein may mediate F-HN interactions. Additionally, destabilizing mutations of PIV5 F that resulted in HN trigger-independent mutant F proteins were identified in a region along the border of F trimer subunits. The positions of the potential HN-interacting region and the region important for F stability in the lower part of the PIV5 F prefusion structure provide clues to the receptor-binding initiated, HN-mediated F trigger.
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