Bovine H5N1 influenza virus binds poorly to human-type sialic acid receptors.
| Autor: | Santos JJS; Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA., Wang S; Department of Molecular Medicine and Department of Immunology and Microbiology, Scripps Research Institute, La Jolla, CA, USA., McBride R; Department of Molecular Medicine and Department of Immunology and Microbiology, Scripps Research Institute, La Jolla, CA, USA., Zhao Y; Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA., Paulson JC; Department of Molecular Medicine and Department of Immunology and Microbiology, Scripps Research Institute, La Jolla, CA, USA., Hensley SE; Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA. |
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| Jazyk: | angličtina |
| Zdroj: | BioRxiv : the preprint server for biology [bioRxiv] 2024 Aug 02. Date of Electronic Publication: 2024 Aug 02. |
| DOI: | 10.1101/2024.08.01.606177 |
| Abstrakt: | Clade 2.3.4.4b highly pathogenic H5N1 avian influenza (HPAI) viruses started circulating widely in lactating dairy cattle in the United States at the end of 2023. Avian influenza viruses enter cells after binding to glycan receptors with terminally linked α2-3 sialic acid, whereas human influenza viruses typically bind to glycan receptors terminally linked α2-6 sialic acid in the upper respiratory tract. Here, we evaluated the receptor binding properties of hemagglutinin (HA) trimers from a clade 2.3.4.4b avian isolate (A/American Wigeon/South Carolina/22-000345-001/2021) and a cattle isolate (A/dairy cattle/Texas/24-008749-002-v/2024). Using two different methods, we found that both of the 2.3.4.4b H5s bound efficiently to glycan receptors with terminally linked α2-3 sialic acid with no detectable binding to glycan receptors with terminally linked α2-6 sialic acid. Our data suggest that clade 2.3.4.4b H5N1 viruses bind poorly to human receptors. It will be important to continue evaluating receptor binding properties of these viruses as they evolve in cattle. Competing Interests: Conflict of Interest S.E.H reports receiving consulting fees from Sanofi, Pfizer, Lumen, Novavax, and Merck. The authors declare no other competing interests. |
| Databáze: | MEDLINE |
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