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

TitleCharacterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site
Authors
KeywordsH4N2
Low pathogenic avian influenza
Multibasic cleavage site
Outbreak
Quail
Issue Date2014
Citation
Virology, 2014, v. 468-470, p. 72-80 How to Cite?
AbstractThe 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. © 2014 Elsevier Inc.
Persistent Identifierhttp://hdl.handle.net/10722/311986
ISSN
2023 Impact Factor: 2.8
2023 SCImago Journal Rankings: 0.838
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWong, Sook San-
dc.contributor.authorYoon, Sun Woo-
dc.contributor.authorZanin, Mark-
dc.contributor.authorSong, Min Suk-
dc.contributor.authorOshansky, Christine-
dc.contributor.authorZaraket, Hassan-
dc.contributor.authorSonnberg, Stephanie-
dc.contributor.authorRubrum, Adam-
dc.contributor.authorSeiler, Patrick-
dc.contributor.authorFerguson, Angela-
dc.contributor.authorKrauss, Scott-
dc.contributor.authorCardona, Carol-
dc.contributor.authorWebby, Richard J.-
dc.contributor.authorCrossley, Beate-
dc.date.accessioned2022-04-06T04:31:55Z-
dc.date.available2022-04-06T04:31:55Z-
dc.date.issued2014-
dc.identifier.citationVirology, 2014, v. 468-470, p. 72-80-
dc.identifier.issn0042-6822-
dc.identifier.urihttp://hdl.handle.net/10722/311986-
dc.description.abstractThe 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. © 2014 Elsevier Inc.-
dc.languageeng-
dc.relation.ispartofVirology-
dc.subjectH4N2-
dc.subjectLow pathogenic avian influenza-
dc.subjectMultibasic cleavage site-
dc.subjectOutbreak-
dc.subjectQuail-
dc.titleCharacterization of an H4N2 influenza virus from Quails with a multibasic motif in the hemagglutinin cleavage site-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.virol.2014.07.048-
dc.identifier.pmid25151061-
dc.identifier.scopuseid_2-s2.0-84906482809-
dc.identifier.volume468-470-
dc.identifier.spage72-
dc.identifier.epage80-
dc.identifier.eissn1096-0341-
dc.identifier.isiWOS:000344434400009-

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