Show simple item record

dc.contributor.authorZaitsev, Viatcheslav
dc.contributor.authorvon Itzstein, Mark
dc.contributor.authorGroves, Darrin
dc.contributor.authorKiefel, Milton
dc.contributor.authorTakimoto, Toru
dc.contributor.authorPortner, Allen
dc.contributor.authorTaylor, Garry
dc.contributor.editorThomas E Shenk, Lynn W Enquist
dc.date.accessioned2017-09-06T05:24:10Z
dc.date.available2017-09-06T05:24:10Z
dc.date.issued2004
dc.date.modified2009-10-19T05:23:54Z
dc.identifier.issn0022538Xen_US
dc.identifier.doi10.1128/JVI.78.7.3733-3741.2004en_US
dc.identifier.urihttp://hdl.handle.net/10072/5051
dc.description.abstractParamyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein, the hemagglutinin-neuraminidase (HN), that is involved in attachment to sialic acid receptors, promotion of fusion, and removal of sialic acid from infected cells and progeny virions. Previously we showed that Newcastle disease virus (NDV) HN contained a pliable sialic acid recognition site that could take two states, a binding state and a catalytic state. Here we present evidence for a second sialic acid binding site at the dimer interface of HN and present a model for its involvement in cell fusion. Three different crystal forms of NDV HN now reveal identical tetrameric arrangements of HN monomers, perhaps indicative of the tetramer association found on the viral surface.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherAmerican Society for Microbiologyen_US
dc.publisher.placeUSAen_US
dc.relation.ispartofpagefrom3733en_US
dc.relation.ispartofpageto3741en_US
dc.relation.ispartofeditionAprilen_US
dc.relation.ispartofissue7en_US
dc.relation.ispartofjournalJournal of Virologyen_US
dc.relation.ispartofvolume78en_US
dc.subject.fieldofresearchcode250105en_US
dc.subject.fieldofresearchcode250301en_US
dc.titleSecond sialic acid binding site in Newcastle Disease virus hemagglutinin-neuraminidase: implications for fusionen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
dc.description.versionPublisheden_US
gro.rights.copyrightCopyright 2004 American Society for Microbiology. The attached file is reproduced here in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.en_US
gro.date.issued2004
gro.hasfulltextFull Text


Files in this item

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record