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Journal of Virology, August 2009, p. 7779-7782, Vol. 83, No. 15
0022-538X/09/$08.00+0 doi:10.1128/JVI.00536-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Yongqi Yan,1,
Aruna Panda,2
Peter L. Collins,3 and
Siba K. Samal1*
Virginia-Maryland Regional College of Veterinary Medicine, University of Maryland, College Park, Maryland 20742,1 Department of Pathology, University of Maryland School of Medicine, Baltimore, Maryland 21201,2 Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 208923
Received 15 March 2009/ Accepted 11 May 2009
The hemagglutinin-neuraminidase (HN) protein of Newcastle disease virus (NDV) is a multifunctional protein that plays a crucial role in virus infectivity. In this study, using the mesogenic strain Beaudette C (BC), we mutated three conserved amino acids thought to be part of the binding/catalytic active site in the HN protein. We also mutated five additional residues near the proposed active site that are nonconserved between BC and the avirulent strain LaSota. The eight recovered NDV HN mutants were assessed for effects on biological activities. While most of the mutations had surprisingly little effect, mutation at conserved residue Y526 reduced the neuraminidase, receptor binding, and fusion activities and attenuated viral virulence in eggs and young birds.
Published ahead of print on 27 May 2009.
These authors contributed equally to the work presented in this study.
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