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J. Biol. Chem., Vol. 281, Issue 8, 5169-5177, February 24, 2006

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Structural and Functional Insights into the Interaction of Echoviruses and Decay-accelerating Factor^*

David M. Pettigrew¹, David T. Williams², David Kerrigan², David J. Evans, Susan M. Lea³, and David Bhella^¶4

From the ^¶Medical Research Council Virology Unit and the Division of Infection and Immunity, Institute of Biomedical and Life Sciences, University of Glasgow, Church Street, Glasgow G11 5JR, Scotland, United Kingdom and the Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom

Many enteroviruses bind to the complement control protein decay-accelerating factor (DAF) to facilitate cell entry. We present here a structure for echovirus (EV) type 12 bound to DAF using cryo-negative stain transmission electron microscopy and three-dimensional image reconstruction to 16-Å resolution, which we interpreted using the atomic structures of EV11 and DAF. DAF binds to a hypervariable region of the capsid close to the 2-fold symmetry axes in an interaction that involves mostly the short consensus repeat 3 domain of DAF and the capsid protein VP2. A bulge in the density for the short consensus repeat 3 domain suggests that a loop at residues 174-180 rearranges to prevent steric collision between closely packed molecules at the 2-fold symmetry axes. Detailed analysis of receptor interactions between a variety of echoviruses and DAF using surface plasmon resonance and comparison of this structure (and our previous work; Bhella, D., Goodfellow, I. G., Roversi, P., Pettigrew, D., Chaudhry, Y., Evans, D. J., and Lea, S. M. (2004) J. Biol. Chem. 279, 8325-8332) with reconstructions published for EV7 bound to DAF support major differences in receptor recognition among these viruses. However, comparison of the electron density for the two virus·receptor complexes (rather than comparisons of the pseudo-atomic models derived from fitting the coordinates into these densities) suggests that the dramatic differences in interaction affinities/specificities may arise from relatively subtle structural differences rather than from large-scale repositioning of the receptor with respect to the virus surface.

Received for publication, September 21, 2005 , and in revised form, November 2, 2005.

The atomic coordinates and structure factors (code 2C8I) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

The three-dimensional reconstructions have been deposited in the Electron Microscopy Data Bank with accession numbers 1182 and 1183.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental figure and a QuickTime movie of the quasi-atomic model.

¹ Supported by a Medical Research Council studentship to S. M. L.

² Supported by a Medical Research Council grant to D. J. E.

³ Supported by Grant REF B16601 from the Biotechnology and Biological Sciences Research Council. To whom correspondence may be addressed. Tel.: 44-1865-275-181; Fax: 44-1865-275-182; E-mail: susan.lea{at}biop.ox.ac.uk.

⁴ Supported by the Medical Research Council. To whom correspondence may be addressed. Tel.: 44-141-330-2988; Fax: 44-141-337-2236; E-mail d.bhella{at}vir.gla.ac.uk.

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