ArticleGlycobiology2022
Wild and domestic animals variably display Neu5Ac and Neu5Gc sialic acids.
Article in Glycobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- The receptor landscape of influenza A viruses.Journal of virology · 2026Review
- Simultaneous ManNAc and Neu5Ac Quantification in Human Sera by LC-MS/MS.International journal of molecular sciences · 2026Article
- Sialic acid serves as a functional receptor for grass carp reovirus.PLoS pathogens · 2025Article
- The sweet side of H5N1 influenza virus infection.PLoS pathogens · 2025Article
- A single mutation in dairy cow-associated H5N1 viruses increases receptor binding breadth.Nature communications · 2024Article
- The mammary glands of cows abundantly display receptors for circulating avian H5 viruses.Journal of virology · 2024Article
- ComplexJournal of virology · 2024Article
- Influenza D virus utilizes both 9-Journal of virology · 2024Article
- The avian influenza A virus receptor SA-α2,3-Gal is expressed in the porcine nasal mucosa sustaining the pig as a mixing vessel for new influenza viruses.Virus research · 2024Article
- A Monocytic Barrier to the Humanization of Immunodeficient Mice.Current stem cell research & therapy · 2024Review
- Influence of Host Sialic Acid Receptors Structure on the Host Specificity of Influenza Viruses.Viruses · 2022Review
- Influence of glycosylation on the immunogenicity and antigenicity of viral immunogens.Biotechnology advancesReview
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialic acids are used as a receptor by several viruses and variations in the linkage type or C-5 modifications affect the binding properties. A species barrier for multiple viruses is present due to α2,3- or α2,6-linked sialic acids. The C-5 position of the sialic acid can be modified to form N-acetylneuraminic acid (Neu5Ac) or N-glycolylneuraminic acid (Neu5Gc), which acts as a determinant for host susceptibility for pathogens such as influenza A virus, rotavirus, and transmissible gastroenteritis coronavirus. Neu5Gc is present in most mammals such as pigs and horses but is absent in humans, ferrets, and dogs. However, little is known about C-5 content in wildlife species or how many C-5 modified sialic acids are present on N-linked glycans or glycolipids. Using our previously developed tissue microarray system, we investigated how 2 different lectins specific for Neu5Gc can result in varying detection levels of Neu5Gc glycans. We used these lectins to map Neu5Gc content in wild Suidae, Cervidae, tigers, and European hedgehogs. We show that Neu5Gc content is highly variable among different species. Furthermore, the removal of N-linked glycans reduces the binding of both Neu5Gc lectins while retention of glycolipids by omitting methanol treatment of tissues increases lectin binding. These findings highlight the importance of using multiple Neu5Gc lectins as the rich variety in which Neu5Gc is displayed can hardly be detected by a single lectin.
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