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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\u2013electron 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 na\u00efve to these viruses.<\/jats:p>","DOI":"10.1126\/sciadv.ady8610","type":"journal-article","created":{"date-parts":[[2025,8,22]],"date-time":"2025-08-22T17:58:56Z","timestamp":1755885536000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":1,"title":["Characterization of the glycoproteins of fish and amphibian influenza B\u2013like viruses"],"prefix":"10.1126","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5848-2741","authenticated-orcid":true,"given":"Gagandeep","family":"Singh","sequence":"first","affiliation":[{"name":"Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA."},{"name":"Center for Vaccine Research and Pandemic Preparedness (C-VaRPP), Icahn School of Medicine at Mount Sinai, New York, NY, 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