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

3 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

Fingerprint

Keywords

H4N2
Low pathogenic avian influenza
Multibasic cleavage site
Outbreak
Quail

ASJC Scopus subject areas

Virology

Cite this

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

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.

@article{4239ea312c5c489286f4df284421e905,

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

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.",

keywords = "H4N2, Low pathogenic avian influenza, Multibasic cleavage site, Outbreak, Quail",

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

year = "2014",

doi = "10.1016/j.virol.2014.07.048",

language = "English (US)",

volume = "468-470",

pages = "72--80",

journal = "Virology",

issn = "0042-6822",

publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Characterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site

AU - Wong, Sook San

AU - Yoon, Sun Woo

AU - Zanin, Mark

AU - Song, Min Suk

AU - Oshansky, Christine

AU - Zaraket, Hassan

AU - Sonnberg, Stephanie

AU - Rubrum, Adam

AU - Seiler, Patrick

AU - Ferguson, Angela

AU - Krauss, Scott

AU - Cardona, Carol

AU - Webby, Richard J.

AU - Crossley, Beate

PY - 2014

Y1 - 2014

N2 - 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.

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.

KW - H4N2

KW - Low pathogenic avian influenza

KW - Multibasic cleavage site

KW - Outbreak

KW - Quail

UR - http://www.scopus.com/inward/record.url?scp=84906482809&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84906482809&partnerID=8YFLogxK

U2 - 10.1016/j.virol.2014.07.048

DO - 10.1016/j.virol.2014.07.048

M3 - Article

C2 - 25151061

AN - SCOPUS:84906482809

VL - 468-470

SP - 72

EP - 80

JO - Virology

JF - Virology

SN - 0042-6822

ER -

Access to Document

10.1016/j.virol.2014.07.048