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Journal of Virology, February 2001, p. 1918-1927, Vol. 75, No. 4
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.4.1918-1927.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Structural and Functional Relationship between the Receptor Recognition and Neuraminidase Activities of the Newcastle Disease Virus Hemagglutinin-Neuraminidase Protein: Receptor Recognition Is Dependent on Neuraminidase Activity

Ronald M. Iorio,1,* Gisela M. Field,1,2 Jennifer M. Sauvron,1,2 Anne M. Mirza,1 Ruitang Deng,1,dagger Paul J. Mahon,3 and Johannes P. Langedijk4

Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655-01221; Department of Biology and Biotechnology, Worcester Polytechnic Institute, Worcester, Massachusetts 016092; Department of Biology, Assumption College, Worcester, Massachusetts 016153; and Department of Mammalian Virology, The Institute for Animal Science and Health (ID-DLO), Lelystad, The Netherlands4

Received 5 September 2000/Accepted 20 November 2000

The terminal globular domain of the paramyxovirus hemagglutinin-neuraminidase (HN) glycoprotein spike has a number of conserved residues that are predicted to form its neuraminidase (NA) active site, by analogy to the influenza virus neuraminidase protein. We have performed a site-directed mutational analysis of the role of these residues in the functional activity of the Newcastle disease virus (NDV) HN protein. Substitutions for several of these residues result in a protein lacking both detectable NA and receptor recognition activity. Contribution of NA activity, either exogenously or by coexpression with another HN protein, partially rescues the receptor recognition activity of these proteins, indicating that the receptor recognition deficiencies of the mutated HN proteins result from their lack of detectable NA activity. In addition to providing support for the homology-based predictions for the structure of HN, these findings argue that (i) the HN residues that mediate its NA activity are not critical to its attachment function and (ii) NA activity is required for the protein to mediate binding to receptors.

* Corresponding author. Mailing address: Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Ave., No., Worcester, MA 01655-0122. Phone: (508) 856-5257. Fax: (508) 856-5920. E-mail: Ronald.Iorio{at}umassmed.edu.

dagger Present address: Molecular & Cellular Virology, Animal Health Biological Discovery, Central Research Division, Pfizer Inc., Groton, CT 06340.

Journal of Virology, February 2001, p. 1918-1927, Vol. 75, No. 4
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.4.1918-1927.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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