{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Singh G"],"funding":["NIAID NIH HHS","NCI NIH HHS","ORFDO NIH HHS"],"pagination":["eady8610"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12372866"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(34)"],"pubmed_abstract":["Influenza-like virus sequences previously identified in fish and amphibians cluster as a sister clade of influenza B viruses but remain largely uncharacterized. We demonstrate that salamander influenza-like virus (SILV) hemagglutinin (HA) is functionally divergent from influenza B virus HA and does not bind to α2,3- and α2,6-linked sialic acids. However, the HAs of Siamese algae-eater influenza-like virus (SAEILV) and chum salmon influenza-like virus (CSILV) bind to α2,3-linked sialic acid. Furthermore, SAEILV HA binds to sialyated Lewis X, is activated by human airway enzymes, and is fusogenic over a broad pH range. SAEILV neuraminidase (NA) has a highly conserved active site and a similar structure to other known NAs. We also determined the cryo-electron microscopy structure of the HA of a previously described virus from the same sister clade, the Wuhan spiny eel influenza virus (WSEIV). No cross-reactive antibodies against these HAs or NAs were found in human serum, suggesting that humans are immunologically naïve to these viruses."],"journal":["Science advances"],"pubmed_title":["Characterization of the glycoproteins of fish and amphibian influenza B-like viruses."],"pmcid":["PMC12372866"],"funding_grant_id":["75N93021C00014","75N93019C00051","R01 AI165692","75N91019C00051","75N99019C00051"],"pubmed_authors":["Singh G","Boons GJ","Krammer F","Bhavsar D","Huang J","Simon V","de Vries RP","Han J","Ferguson JA","Ward A","Vasilev K"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of the glycoproteins of fish and amphibian influenza B-like viruses.","description":"Influenza-like virus sequences previously identified in fish and amphibians cluster as a sister clade of influenza B viruses but remain largely uncharacterized. We demonstrate that salamander influenza-like virus (SILV) hemagglutinin (HA) is functionally divergent from influenza B virus HA and does not bind to α2,3- and α2,6-linked sialic acids. However, the HAs of Siamese algae-eater influenza-like virus (SAEILV) and chum salmon influenza-like virus (CSILV) bind to α2,3-linked sialic acid. Furthermore, SAEILV HA binds to sialyated Lewis X, is activated by human airway enzymes, and is fusogenic over a broad pH range. SAEILV neuraminidase (NA) has a highly conserved active site and a similar structure to other known NAs. We also determined the cryo-electron microscopy structure of the HA of a previously described virus from the same sister clade, the Wuhan spiny eel influenza virus (WSEIV). No cross-reactive antibodies against these HAs or NAs were found in human serum, suggesting that humans are immunologically naïve to these viruses.","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-07-15T14:21:18.108Z","creation":"2026-07-05T03:11:57.04Z"},"accession":"S-EPMC12372866","cross_references":{"pubmed":["40845102"],"doi":["10.1126/sciadv.ady8610"]}}