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Sci Adv . Characterization of the glycoproteins of fish and amphibian influenza B-like viruses

tetano

Editor, Senior Moderator
Sci Adv


. 2025 Aug 22;11(34):eady8610.
doi: 10.1126/sciadv.ady8610. Epub 2025 Aug 22. Characterization of the glycoproteins of fish and amphibian influenza B-like viruses

Gagandeep Singh[SUP] 1 2 [/SUP], Jiachen Huang[SUP] 3 [/SUP], Disha Bhavsar[SUP] 1 2 [/SUP], Kirill Vasilev[SUP] 1 2 [/SUP], James A Ferguson[SUP] 3 [/SUP], Geert-Jan Boons[SUP] 4 5 [/SUP], Viviana Simon[SUP] 1 2 6 7 8 [/SUP], Robert P de Vries[SUP] 4 [/SUP], Julianna Han[SUP] 3 [/SUP], Andrew Ward[SUP] 3 [/SUP], Florian Krammer[SUP] 1 2 6 9 [/SUP]



Affiliations
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.


 
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