Characterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site

Sook San Wong; Sun Woo Yoon; Mark Zanin; Min Suk Song; Christine Oshansky; Hassan Zaraket; Stephanie Sonnberg; Adam Rubrum; Patrick Seiler; Angela Ferguson; Scott Krauss; Carol Cardona; Richard J. Webby; Beate Crossley

doi:10.1016/j.virol.2014.07.048

Characterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site

Sook San Wong, Sun Woo Yoon, Mark Zanin, Min Suk Song, Christine Oshansky, Hassan Zaraket, Stephanie Sonnberg, Adam Rubrum, Patrick Seiler, Angela Ferguson, Scott Krauss, Carol Cardona, Richard J. Webby, Beate Crossley

California Animal Health & Food Safety Lab

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

The cleavage motif in the hemagglutinin (HA) protein of highly pathogenic H5 and H7 subtypes of avian influenza viruses is characterized by a peptide insertion or a multibasic cleavage site (MBCS). Here, we isolated an H4N2 virus from quails (Quail/CA12) with two additional arginines in the HA cleavage site, PEK. RRTR/G, forming an MBCS-like motif. Quail/CA12 is a reassortant virus with the HA and neuraminidase (NA) gene most similar to a duck-isolated H4N2 virus, PD/CA06 with a monobasic HA cleavage site. Quail/CA12 required exogenous trypsin for efficient growth in culture and caused no clinical illness in infected chickens. Quail/CA12 had high binding preference for α2,6-linked sialic acids and showed higher replication and transmission ability in chickens and quails than PD/CA06. Although the H4N2 virus remained low pathogenic, these data suggests that the acquisition of MBCS in the field is not restricted to H5 or H7 subtypes.

Original language	English (US)
Pages (from-to)	72-80
Number of pages	9
Journal	Virology
Volume	468-470
DOIs	https://doi.org/10.1016/j.virol.2014.07.048
State	Published - 2014

Keywords

H4N2
Low pathogenic avian influenza
Multibasic cleavage site
Outbreak
Quail

ASJC Scopus subject areas

Virology

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10.1016/j.virol.2014.07.048

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Wong, S. S., Yoon, S. W., Zanin, M., Song, M. S., Oshansky, C., Zaraket, H., Sonnberg, S., Rubrum, A., Seiler, P., Ferguson, A., Krauss, S., Cardona, C., Webby, R. J., & Crossley, B. (2014). Characterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site. Virology, 468-470, 72-80. https://doi.org/10.1016/j.virol.2014.07.048

Characterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site. / Wong, Sook San; Yoon, Sun Woo; Zanin, Mark; Song, Min Suk; Oshansky, Christine; Zaraket, Hassan; Sonnberg, Stephanie; Rubrum, Adam; Seiler, Patrick; Ferguson, Angela; Krauss, Scott; Cardona, Carol; Webby, Richard J.; Crossley, Beate.

In: Virology, Vol. 468-470, 2014, p. 72-80.

Research output: Contribution to journal › Article › peer-review

Wong, Sook San ; Yoon, Sun Woo ; Zanin, Mark ; Song, Min Suk ; Oshansky, Christine ; Zaraket, Hassan ; Sonnberg, Stephanie ; Rubrum, Adam ; Seiler, Patrick ; Ferguson, Angela ; Krauss, Scott ; Cardona, Carol ; Webby, Richard J. ; Crossley, Beate. / Characterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site. In: Virology. 2014 ; Vol. 468-470. pp. 72-80.

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abstract = "The cleavage motif in the hemagglutinin (HA) protein of highly pathogenic H5 and H7 subtypes of avian influenza viruses is characterized by a peptide insertion or a multibasic cleavage site (MBCS). Here, we isolated an H4N2 virus from quails (Quail/CA12) with two additional arginines in the HA cleavage site, PEK. RRTR/G, forming an MBCS-like motif. Quail/CA12 is a reassortant virus with the HA and neuraminidase (NA) gene most similar to a duck-isolated H4N2 virus, PD/CA06 with a monobasic HA cleavage site. Quail/CA12 required exogenous trypsin for efficient growth in culture and caused no clinical illness in infected chickens. Quail/CA12 had high binding preference for α2,6-linked sialic acids and showed higher replication and transmission ability in chickens and quails than PD/CA06. Although the H4N2 virus remained low pathogenic, these data suggests that the acquisition of MBCS in the field is not restricted to H5 or H7 subtypes.",

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AU - Song, Min Suk

AU - Oshansky, Christine

AU - Zaraket, Hassan

AU - Sonnberg, Stephanie

AU - Rubrum, Adam

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AU - Ferguson, Angela

AU - Krauss, Scott

AU - Cardona, Carol

AU - Webby, Richard J.

AU - Crossley, Beate

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AB - The cleavage motif in the hemagglutinin (HA) protein of highly pathogenic H5 and H7 subtypes of avian influenza viruses is characterized by a peptide insertion or a multibasic cleavage site (MBCS). Here, we isolated an H4N2 virus from quails (Quail/CA12) with two additional arginines in the HA cleavage site, PEK. RRTR/G, forming an MBCS-like motif. Quail/CA12 is a reassortant virus with the HA and neuraminidase (NA) gene most similar to a duck-isolated H4N2 virus, PD/CA06 with a monobasic HA cleavage site. Quail/CA12 required exogenous trypsin for efficient growth in culture and caused no clinical illness in infected chickens. Quail/CA12 had high binding preference for α2,6-linked sialic acids and showed higher replication and transmission ability in chickens and quails than PD/CA06. Although the H4N2 virus remained low pathogenic, these data suggests that the acquisition of MBCS in the field is not restricted to H5 or H7 subtypes.

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Characterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site

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Keywords

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