ArticleNature communications2021
In situ structure and organization of the influenza C virus surface glycoprotein.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Membrane Fusion-Inspired Nanomaterials: Emerging Strategies for Infectious Disease and Cancer Diagnostics.Advanced healthcare materials · 2026Review
- Differential tissue tropism and transmission efficiency of two dominant influenza D clades with overlapping but distinct receptor binding fine specificities in ferrets.PLoS pathogens · 2025Article
- Virion motility of sialoglycan-cleaving respiratory viruses.Npj viruses · 2025Review
- Intranasal administration of a panreactive influenza antibody reveals Fc-independent mode of protection.Scientific reports · 2025Article
- The virucidal potential effects of violet-blue light on influenza D virus.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025Article
- The nanoscale organization of the Nipah virus fusion protein informs new membrane fusion mechanisms.eLife · 2025Article
- Advantages of Broad-Spectrum Influenza mRNA Vaccines and Their Impact on Pulmonary Influenza.Vaccines · 2024Review
- Assembly of respiratory syncytial virus matrix protein lattice and its coordination with fusion glycoprotein trimers.Nature communications · 2024Article
- Antibody inhibition of influenza A virus assembly and release.Journal of virology · 2024Article
- The Art of Viral Membrane Fusion and Penetration.Sub-cellular biochemistry · 2023Article
- Temporal and Gene Reassortment Analysis of Influenza C Virus Outbreaks in Hong Kong, SAR, China.Journal of virology · 2022Article
- Detecting in-solution conformational changes in viral fusogens using tryptophan-induced fluorescence quenching.STAR protocols · 2021Article
- Host Range, Biology, and Species Specificity of Seven-Segmented Influenza Viruses-A Comparative Review on Influenza C and D.Pathogens (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
The lipid-enveloped influenza C virus contains a single surface glycoprotein, the haemagglutinin-esterase-fusion (HEF) protein, that mediates receptor binding, receptor destruction, and membrane fusion at the low pH of the endosome. Here we apply electron cryotomography and subtomogram averaging to describe the structural basis for hexagonal lattice formation by HEF on the viral surface. The conformation of the glycoprotein in situ is distinct from the structure of the isolated trimeric ectodomain, showing that a splaying of the membrane distal domains is required to mediate contacts that form the lattice. The splaying of these domains is also coupled to changes in the structure of the stem region which is involved in membrane fusion, thereby linking HEF's membrane fusion conformation with its assembly on the virus surface. The glycoprotein lattice can form independent of other virion components but we show a major role for the matrix layer in particle formation.
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Registered trials
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.