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Journal of Virology, September 2004, p. 9051-9063, Vol. 78, No. 17
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.17.9051-9063.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Measles Virus (MV) Hemagglutinin: Evidence that Attachment Sites for MV Receptors SLAM and CD46 Overlap on the Globular Head

Nicolas Massé,1 Michelle Ainouze,1 Benjamin Néel,1 T. Fabian Wild,2 Robin Buckland,1* and Johannes P. M. Langedijk3

Molecular Basis of Paramyxovirus Entry,1 Immunobiology of Viral infections, INSERM U404, Immunité et Vaccination, CERVI, IFR 128 Biosciences Lyon-Gerland, Lyon, France,2 Pepscan Systems Inc., Lelystad, The Netherlands3

Received 19 February 2004/ Accepted 20 April 2004

Measles virus hemagglutinin (MVH) residues potentially responsible for attachment to the wild-type (wt) MV receptor SLAM (CD150) have been identified and localized on the MVH globular head by reference to a revised hypothetical structural model for MVH (www.pepscan.nl/downloads/measlesH.pdb). We show that the mutation of five charged MVH residues which are conserved among morbillivirus H proteins has major effects on both SLAM downregulation and SLAM-dependent fusion. In the three-dimensional surface representation of the structural model, three of these residues (D505, D507, and R533) align the rim on one side of the cavity on the top surface of the MVH globular head and form the basis of a single continuous site that overlaps with the 546-548-549 CD46 binding site. We show that the overlapping sites fall within the footprint of an anti-MVH monoclonal antibody that neutralizes both wt and laboratory-vaccine MV strains and whose epitope contains R533. Our study does not exclude the possibility that Y481 binds CD46 directly but suggests that the N481Y mutation of wt MVH could influence, at a distance, the conformation of the overlapping sites so that affinity to CD46 increases. The relevance of these results to present concepts of MV receptor usage is discussed, and an explanation is proposed as to why morbillivirus attachment proteins are H, whereas those from the other paramyxoviruses are HN (hemagglutinin-neuraminidase).

* Corresponding author. Mailing address: INSERM U404, CERVI, IFR 128 Biosciences Lyon-Gerland, 21 Ave. Tony Garnier, 69365 Lyon Cedex 07, France. Phone: 33.4.37.28.23.93. Fax: 33.4.37.28.23.91. E-mail: buckland{at}cervi-lyon.inserm.fr.

Journal of Virology, September 2004, p. 9051-9063, Vol. 78, No. 17
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.17.9051-9063.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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