{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Singh G"],"funding":["NIAID NIH HHS","NCI NIH HHS","ORFDO NIH HHS"],"pubmed_abstract":["Novel influenza-like virus sequences previously identified in fish and amphibians were found to cluster as a sister clade of influenza B viruses, but have thus far remained uncharacterized. We demonstrate that salamander influenza-like virus (SILV) HA is functionally divergent from influenza B virus HA and does not bind to α 2,3- 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 at a wide range of pH conditions. SAEILV 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). Importantly, no cross-reactive antibodies against these HAs or NAs were found in the human serum, suggesting that humans are immunologically naïve to these viruses."],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.05.08.652883"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12247948"],"repository":["biostudies-literature"],"pubmed_title":["Characterization of the glycoproteins of novel fish influenza B-like viruses."],"pmcid":["PMC12247948"],"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 novel fish influenza B-like viruses.","description":"Novel influenza-like virus sequences previously identified in fish and amphibians were found to cluster as a sister clade of influenza B viruses, but have thus far remained uncharacterized. We demonstrate that salamander influenza-like virus (SILV) HA is functionally divergent from influenza B virus HA and does not bind to α 2,3- 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 at a wide range of pH conditions. SAEILV 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). Importantly, no cross-reactive antibodies against these HAs or NAs were found in the human serum, suggesting that humans are immunologically naïve to these viruses.","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-04-08T09:55:55.448Z","creation":"2025-08-23T03:09:33.055Z"},"accession":"S-EPMC12247948","cross_references":{"pubmed":["40654808"],"doi":["10.1101/2025.05.08.652883"]}}