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Journal of Virology, April 2004, p. 3733-3741, Vol. 78, No. 7
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.7.3733-3741.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Second Sialic Acid Binding Site in Newcastle Disease Virus Hemagglutinin-Neuraminidase: Implications for Fusion

Viatcheslav Zaitsev,1 Mark von Itzstein,2 Darrin Groves,2 Milton Kiefel,2 Toru Takimoto,3 Allen Portner,3 and Garry Taylor1*

Centre for Biomolecular Sciences, University of St. Andrews, St. Andrews, Fife KY16 9ST, United Kingdom,1 Institute for Glycomics, Griffith University, Gold Coast City, Queensland 9726, Australia,2 Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105-27943

Received 29 October 2003/ Accepted 4 December 2003

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.

* Corresponding author. Mailing address: Centre for Biomolecular Sciences, University of St. Andrews, St. Andrews, Fife KY16 9ST, United Kingdom. Phone: 44 1334 467301. Fax: 44 1334 467301. E-mail: glt2{at}st-andrews.ac.uk.

Journal of Virology, April 2004, p. 3733-3741, Vol. 78, No. 7
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.7.3733-3741.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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