Characterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site
2014
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
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, PEKRRTR/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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