H2N2V1, Main, Exploration, bibRecord, 000738

Characterization of an H4N2 Influenza Virus from Quails with a Multibasic Motif in the Hemagglutinin Cleavage Site

Identifieur interne : 000738 ( Main/Exploration ); précédent : 000737; suivant : 000739

Characterization of an H4N2 Influenza Virus from Quails with a Multibasic Motif in the Hemagglutinin Cleavage Site

Auteurs : Sook-San Wong ; Sun-Woo Yoon [Corée du Sud] ; Mark Zanin ; Min-Suk Song ; Christine Oshansky ; Hassan Zaraket [Liban] ; Stephanie Sonnberg ; Adam Rubrum ; Patrick Seiler ; Angela Ferguson ; Scott Krauss ; Carol Cardona ; Richard J. Webby ; Beate Crossley

Source :

Virology [ 0042-6822 ] ; 2014.

RBID : PMC:4253870

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, 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.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4253870

DOI: 10.1016/j.virol.2014.07.048
PubMed: 25151061
PubMed Central: 4253870

Affiliations:

Corée du Sud, Liban

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p id="P2">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<bold>RR</bold>
TR/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.</p>
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Characterization of an H4N2 Influenza Virus from Quails with a Multibasic Motif in the Hemagglutinin Cleavage Site

Characterization of an H4N2 Influenza Virus from Quails with a Multibasic Motif in the Hemagglutinin Cleavage Site

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Abstract

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