ArticlemSphere
Distribution of O-Acetylated Sialic Acids among Target Host Tissues for Influenza Virus.
Article in mSphere. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
56 citing papers in PubMed, 78 citations in OpenAlex.
- Delayed antiviral immune response in alveolar type 2 cells increases susceptibility to influenza virus in alveoli.Chinese medical journal · 2026Article
- Targeting virus-glycan recognition in influenza viruses and coronaviruses: from the molecular principles to glycomimetic antivirals strategies.RSC chemical biology · 2026Review
- Article
- OC43 clinical isolate spike proteins have distinct carbohydrate-binding properties.Nature communications · 2026Article
- Evaluation of the Therapeutic Potential of Natural Peptides Against Hemagglutinin-Esterase of Bovine Coronavirus Based on Molecular Dynamics Simulation Studies.Veterinary medicine international · 2026Article
- Spatial mapping of influenza and coronavirus receptors in the respiratory and intestinal tract epithelium of beef cattle using advanced PixF image analysis.Scientific reports · 2025Article
- Advancing influenza virus treatment:Materials today. Bio · 2025Article
- Article
- 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
- Gastrointestinal Infiltration in Influenza Virus Infection: Mechanisms and Clinical Insights.Viruses · 2025Review
- Loss of sialic acid side-chainProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Extended receptor repertoire of an adenovirus associated with human obesity.PLoS pathogens · 2025Article
- The HCoV-HKU1 N-Terminal Domain Binds a Wide Range of 9-ACS infectious diseases · 2024Article
- Synthetic Sialosides Terminated with 8-N-Substituted Sialic Acid as Selective Substrates for Sialidases from Bacteria and Influenza Viruses.Angewandte Chemie (International ed. in English) · 2024Article
- H19 influenza A virus exhibits species-specific MHC class II receptor usage.Cell host & microbe · 2024Article
- The HCoV-HKU1 N-terminal domain binds a wide range of 9-bioRxiv : the preprint server for biology · 2024Article
- Influenza D virus utilizes both 9-Journal of virology · 2024Article
- Elevated concentrations of Neu5Ac and Neu5,9AcGlycoconjugate journal · 2023Article
- Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry.Nature communications · 2023Article
- Increased public health threat of avian-origin H3N2 influenza virus caused by its evolution in dogs.eLife · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Sialic acids (Sias) are important glycans displayed on the cells and tissues of many different animals and are frequent targets for binding and modification by pathogens, including influenza viruses. Influenza virus hemagglutinins bind Sias during the infection of their normal hosts, while the encoded neuraminidases and/or esterases remove or modify the Sia to allow virion release or to prevent rebinding. Sias naturally occur in a variety of modified forms, and modified Sias can alter influenza virus host tropisms through their altered interactions with the viral glycoproteins. However, the distribution of modified Sia forms and their effects on pathogen-host interactions are still poorly understood. Here we used probes developed from viral Sia-binding proteins to detect O-acetylated (4-O-acetyl, 9-O-acetyl, and 7,9-O-acetyl) Sias displayed on the tissues of some natural or experimental hosts for influenza viruses. These modified Sias showed highly variable displays between the hosts and tissues examined. The 9-O-acetyl (and 7,9-) modified Sia forms were found on cells and tissues of many hosts, including mice, humans, ferrets, guinea pigs, pigs, horses, dogs, as well as in those of ducks and embryonated chicken egg tissues and membranes, although in variable amounts. The 4-O-acetyl Sias were found in the respiratory tissues of fewer animals, being primarily displayed in the horse and guinea pig, but were not detected in humans or pigs. The results suggest that these Sia variants may influence virus tropisms by altering and selecting their cell interactions.
Indexed as
Identifiers
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.