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Journal of Virology, September 2007, p. 9900-9910, Vol. 81, No. 18
0022-538X/07/$08.00+0     doi:10.1128/JVI.00909-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Mutations in the Stalk of the Measles Virus Hemagglutinin Protein Decrease Fusion but Do Not Interfere with Virus-Specific Interaction with the Homologous Fusion Protein{triangledown}

Elizabeth A. Corey1,{dagger} and Ronald M. Iorio1,2*

Department of Molecular Genetics and Microbiology,1 Program in Immunology and Virology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, Massachusetts 016552

Received 27 April 2007/ Accepted 28 June 2007

The hemagglutinin (H) protein of measles virus (MV) mediates attachment to cellular receptors. The ectodomain of the H spike is thought to consist of a membrane-proximal stalk and terminal globular head, in which resides the receptor-binding activity. Like other paramyxovirus attachment proteins, MV H also plays a role in fusion promotion, which is mediated through an interaction with the viral fusion (F) protein. The stalk of the hemagglutinin-neuraminidase (HN) protein of several paramyxoviruses determines specificity for the homologous F protein. In addition, mutations in a conserved domain in the Newcastle disease virus (NDV) HN stalk result in a sharp decrease in fusion and an impaired ability to interact with NDV F in a cell surface coimmunoprecipitation (co-IP) assay. The region of MV H that determines specificity for the F protein has not been identified. Here, we have adapted the co-IP assay to detect the MV H-F complex at the surface of transfected HeLa cells. We have also identified mutations in a domain in the MV H stalk, similar to the one in the NDV HN stalk, that also drastically reduce fusion yet do not block complex formation with MV F. These results indicate that this domain in the MV H stalk is required for fusion but suggest either that mutation of it indirectly affects the H-dependent activation of F or that the MV H-F interaction is mediated by more than one domain in H. This points to an apparent difference in the way the MV and NDV glycoproteins interact to regulate fusion.

* Corresponding author. Mailing address: Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655. Phone: (508) 856-5257. Fax: (508) 856-5920. E-mail: ronald.iorio{at}umassmed.edu

{triangledown} Published ahead of print on 11 July 2007.

{dagger} Present address: The Whitney Laboratory, St. Augustine, FL.

Journal of Virology, September 2007, p. 9900-9910, Vol. 81, No. 18
0022-538X/07/$08.00+0     doi:10.1128/JVI.00909-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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