TY - JOUR
T1 - Functionality of the putative surface glycoproteins of the Wuhan spiny eel influenza virus
AU - Arunkumar, Guha Asthagiri
AU - Bhavsar, Disha
AU - Li, Tiehai
AU - Strohmeier, Shirin
AU - Chromikova, Veronika
AU - Amanat, Fatima
AU - Bunyatov, Mehman
AU - Wilson, Patrick C.
AU - Ellebedy, Ali H.
AU - Boons, Geert Jan
AU - Simon, Viviana
AU - de Vries, Robert P.
AU - Krammer, Florian
N1 - Funding Information:
We would like to thank Andrew Duty and Tom Moran at the Department of Microbiology at the Icahn School of Medicine at Mount Sinai for letting us use their BLI device. We would also like to thank Edward Holmes at The University of Sidney for inspiring us to perform this study and for making the sequence information available. This work was partially funded by NIAID CEIRS contract HHSN272201400008C and NIAID grant R01 AI117287. R.P.dV is a recipient of an ERC Starting Grant from the European Commission (802780) and a Beijerinck Premium of the Royal Dutch Academy of Sciences. Synthesis and microarray analysis were funded by a grant from the Netherlands Organization for Scientific Research (NWO TOPPUNT 718.015.003) to G.-J.B.
Publisher Copyright:
© 2021, The Author(s).
PY - 2021/12/1
Y1 - 2021/12/1
N2 - A panel of influenza virus-like sequences were recently documented in fish and amphibians. Of these, the Wuhan spiny eel influenza virus (WSEIV) was found to phylogenetically cluster with influenza B viruses as a sister clade. Influenza B viruses have been documented to circulate only in humans, with certain virus isolates found in harbor seals. It is therefore interesting that a similar virus was potentially found in fish. Here we characterize the putative hemagglutinin (HA) and neuraminidase (NA) surface glycoproteins of the WSEIV. Functionally, we show that the WSEIV NA-like protein has sialidase activity comparable to B/Malaysia/2506/2004 influenza B virus NA, making it a bona fide neuraminidase that is sensitive to NA inhibitors. We tested the functionality of the HA by addressing the receptor specificity, stability, preferential airway protease cleavage, and fusogenicity. We show highly specific binding to monosialic ganglioside 2 (GM2) and fusogenicity at a range of different pH conditions. In addition, we found limited antigenic conservation of the WSEIV HA and NA relative to the B/Malaysia/2506/2004 virus HA and NA. In summary, we perform a functional and antigenic characterization of the glycoproteins of WSEIV to assess if it is indeed a bona fide influenza virus potentially circulating in ray-finned fish.
AB - A panel of influenza virus-like sequences were recently documented in fish and amphibians. Of these, the Wuhan spiny eel influenza virus (WSEIV) was found to phylogenetically cluster with influenza B viruses as a sister clade. Influenza B viruses have been documented to circulate only in humans, with certain virus isolates found in harbor seals. It is therefore interesting that a similar virus was potentially found in fish. Here we characterize the putative hemagglutinin (HA) and neuraminidase (NA) surface glycoproteins of the WSEIV. Functionally, we show that the WSEIV NA-like protein has sialidase activity comparable to B/Malaysia/2506/2004 influenza B virus NA, making it a bona fide neuraminidase that is sensitive to NA inhibitors. We tested the functionality of the HA by addressing the receptor specificity, stability, preferential airway protease cleavage, and fusogenicity. We show highly specific binding to monosialic ganglioside 2 (GM2) and fusogenicity at a range of different pH conditions. In addition, we found limited antigenic conservation of the WSEIV HA and NA relative to the B/Malaysia/2506/2004 virus HA and NA. In summary, we perform a functional and antigenic characterization of the glycoproteins of WSEIV to assess if it is indeed a bona fide influenza virus potentially circulating in ray-finned fish.
UR - http://www.scopus.com/inward/record.url?scp=85118152079&partnerID=8YFLogxK
U2 - 10.1038/s41467-021-26409-2
DO - 10.1038/s41467-021-26409-2
M3 - Article
C2 - 34697321
AN - SCOPUS:85118152079
SN - 2041-1723
VL - 12
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 6161
ER -