Second sialic acid binding site in Newcastle Disease virus hemagglutinin-neuraminidase: implications for fusion.

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Title Second sialic acid binding site in Newcastle Disease virus hemagglutinin-neuraminidase: implications for fusion.
Author Zaitsev, Viatcheslav; von Itzstein, Mark; Groves, Darrin; Kiefel, Milton; Takimoto, Toru; Portner, Allen; Taylor, Garry
Journal Name Journal of Virology
Editor Thomas E Shenk, Lynn W Enquist
Year Published 2004
Place of publication USA
Publisher American Society for Microbiology
Abstract Paramyxoviruses 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.
Peer Reviewed Yes
Published Yes
Publisher URI http://jvi.asm.org/
Alternative URI http://dx.doi.org/10.1128/JVI.78.7.3733-3741.2004
Volume 78
Issue Number 7
Edition April
Page from 3733
Page to 3741
ISSN 0022-538X
Date Accessioned 2005-03-22
Language en_AU
Research Centre Institute for Glycomics
Faculty Institute for Glycomics
Subject PRE2009-Organic Chemical Synthesis; PRE2009-Structural Chemistry
URI http://hdl.handle.net/10072/5051
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1

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