This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hewat, E. A.
Right arrow Articles by Blaas, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hewat, E. A.
Right arrow Articles by Blaas, D.

 Previous Article  |  Next Article 

J Virol, May 1998, p. 4396-4402, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Structure of a Neutralizing Antibody Bound Monovalently to Human Rhinovirus 2

Elizabeth A. Hewat,1,* Thomas C. Marlovits,2 and Dieter Blaas2

Institut de Biologie Structurale Jean-Pierre Ebel, 38027 Grenoble, France,1 and Institute of Biochemistry, University of Vienna, A-1030 Vienna, Austria2

Received 9 July 1997/Accepted 26 January 1998

The structure of a complex between human rhinovirus 2 (HRV2) and the Fab fragment of neutralizing monoclonal antibody (MAb) 3B10 has been determined to 25-Å resolution by cryoelectron microscopy and three-dimensional reconstruction techniques. The footprint of 3B10 on HRV2 is very similar to that of neutralizing MAb 8F5, which binds bivalently across the icosahedral twofold axis. However, the 3B10 Fab fragment (Fab-3B10) is bound in an orientation, inclined at approximately 45° to the surface of the virus capsid, which is compatible only with monovalent binding of the antibody. The canyon around the fivefold axis is not directly obstructed by the bound Fab. The X-ray structures of a closely related HRV (HRV1A) and a Fab fragment were fitted to the density maps of the HRV2-Fab-3B10 complex obtained by cryoelectron microscope techniques. The footprint of 3B10 on the viral surface is largely on VP2 but also covers the VP3 loop centered on residue 3064 and the VP1 loop centered on residue 1267. MAb 3B10 can interact directly with VP2 residue 2164, the site of an escape mutation on VP2, and with VP1 residues 1264 to 1267, the site of a deletion escape mutation. Deletion of these residues shortens the VP1 loop, moving it away from the MAb binding site. All structural and biochemical evidence indicates that MAb 3B10 binds to a conformation epitope on HRV2.

* Corresponding author. Mailing address: Institut de Biologie Structurale Jean-Pierre Ebel, 41 av. des Martyrs, 38027 Grenoble, France. Phone: (33) 4 76 884568. Fax: (33) 4 76 885494. E-mail: HEWAT{at}IBS.FR.

J Virol, May 1998, p. 4396-4402, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Hafenstein, S., Bowman, V. D., Sun, T., Nelson, C. D. S., Palermo, L. M., Chipman, P. R., Battisti, A. J., Parrish, C. R., Rossmann, M. G. (2009). Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids. J. Virol. 83: 5556-5566 [Abstract] [Full Text]  
  • Baravalle, G., Brabec, M., Snyers, L., Blaas, D., Fuchs, R. (2004). Human Rhinovirus Type 2-Antibody Complexes Enter and Infect Cells via Fc-{gamma} Receptor IIB1. J. Virol. 78: 2729-2737 [Abstract] [Full Text]  
  • Hardy, S. A., Dimmock, N. J. (2002). Valency of Antibody Binding to Enveloped Virus Particles as Determined by Surface Plasmon Resonance. J. Virol. 77: 1649-1652 [Abstract] [Full Text]  
  • Klasse, P. J., Sattentau, Q. J. (2002). Occupancy and mechanism in antibody-mediated neutralization of animal viruses. J. Gen. Virol. 83: 2091-2108 [Abstract] [Full Text]  
  • Baker, T. S., Olson, N. H., Fuller, S. D. (1999). Adding the Third Dimension to Virus Life Cycles: Three-Dimensional Reconstruction of Icosahedral Viruses from Cryo-Electron Micrographs. Microbiol. Mol. Biol. Rev. 63: 862-922 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»