ArticlePLoS pathogens2016
An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 90 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
90 citing papers in PubMed, 121 citations in OpenAlex.
- Detection of Influenza D Virus using Reverse Transcription Loop-Mediated Isothermal Amplification.Emerging infectious diseases · 2026Article
- The receptor landscape of influenza A viruses.Journal of virology · 2026Review
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- Influenza Virus Neuraminidase Glycoprotein, Its Inhibitors, and Their Resistance.Advances in experimental medicine and biology · 2026Review
- Genetic and Phylogenetic Characterization of Influenza D Viruses From South Korean Cattle, 2022-2023.Transboundary and emerging diseases · 2026Article
- The hemagglutinin-like proteins of basal vertebrate influenza-like viruses exhibit sialic-acid receptor binding disparity and their structural bases.PLoS pathogens · 2025Article
- 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
- Seroprevalence of influenza C and D virus infections among cattle in Japan.Veterinary and animal science · 2025Article
- Molecular basis of influenza ribonucleoprotein complex assembly and processive RNA synthesis.Science (New York, N.Y.) · 2025Article
- High Prevalence of Influenza D Virus Infection in Swine, Northern Ireland.Emerging infectious diseases · 2025Article
- Intranasal administration of a panreactive influenza antibody reveals Fc-independent mode of protection.Scientific reports · 2025Article
- The mammary glands of cows abundantly display receptors for circulating avian H5 viruses.Journal of virology · 2024Article
- Rapid evolution leads to extensive genetic diversification of cattle flu Influenza D virus.Communications biology · 2024Article
- Article
- Characterization of Influenza D Virus Reassortant Strain in Swine from Mixed Pig and Beef Farm, France.Emerging infectious diseases · 2024Article
- Antigenic commonality and divergence of hemagglutinin-esterase-fusion protein among influenza D virus lineages revealed using epitope mapping.Journal of virology · 2024Article
- Pathogenesis, Transmission, and Within-Host Evolution of Bovine-Origin Influenza D Virus in Pigs.Transboundary and emerging diseases · 2024Article
- Influenza D in Domestic and Wild Animals.Viruses · 2023Review
- Epidemiological, serological, and genetic evidence of influenza D virus infection in humans: Is it a justifiable cause for concern?Virulence · 2023Article
- Influenza D virus was not detected among prospectively studied swine farm in multiple provinces of China.Influenza and other respiratory viruses · 2023Article
30 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health.
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What OpenQuestion holds
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.