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Journal of Virology, September 2007, p. 9851-9858, Vol. 81, No. 18
0022-538X/07/$08.00+0     doi:10.1128/JVI.00775-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Minute Virus of Mice, a Parvovirus, in Complex with the Fab Fragment of a Neutralizing Monoclonal Antibody{triangledown}

Bärbel Kaufmann,1 Alberto López-Bueno,2,{dagger} Mauricio G. Mateu,2 Paul R. Chipman,1 Christian D. S. Nelson,3 Colin R. Parrish,3 José M. Almendral,2 and Michael G. Rossmann1*

Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, Indiana 47907-2054,1 Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, 28049 Cantoblanco, Madrid, Spain,2 Baker Institute for Animal Health and Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York 148533

Received 10 April 2007/ Accepted 2 July 2007

The structure of virus-like particles of the lymphotropic, immunosuppressive strain of minute virus of mice (MVMi) in complex with the neutralizing Fab fragment of the mouse monoclonal antibody (MAb) B7 was determined by cryo-electron microscopy to 7-Å resolution. The Fab molecule recognizes a conformational epitope at the vertex of a three-fold protrusion on the viral surface, thereby simultaneously engaging three symmetry-related viral proteins in binding. The location of the epitope close to the three-fold axis is consistent with the previous analysis of MVMi mutants able to escape from the B7 antibody. The binding site close to the symmetry axes sterically forbids the binding of more than one Fab molecule per spike. MAb as well as the Fab molecules inhibits the binding of the minute virus of mice (MVM) to permissive cells but can also neutralize MVM postattachment. This finding suggests that the interaction of B7 with three symmetry-related viral subunits at each spike hinders structural transitions in the viral capsid essential during viral entry.

* Corresponding author. Mailing address: Department of Biological Sciences, Purdue University, 915 W. State St., West Lafayette, IN 47907-2054. Phone: (765) 494-4911. Fax: (765) 496-1189. E-mail: mr{at}purdue.edu

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

{dagger} Present address: Centro Nacional de Biotecnología (CSIC-UAM), 28049 Cantoblanco, Madrid, Spain.

Journal of Virology, September 2007, p. 9851-9858, Vol. 81, No. 18
0022-538X/07/$08.00+0     doi:10.1128/JVI.00775-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kaufmann, B., Chipman, P. R., Kostyuchenko, V. A., Modrow, S., Rossmann, M. G. (2008). Visualization of the Externalized VP2 N Termini of Infectious Human Parvovirus B19. J. Virol. 82: 7306-7312 [Abstract] [Full Text]  


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