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J. Biol. Chem., Vol. 279, Issue 9, 8325-8332, February 27, 2004

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The Structure of Echovirus Type 12 Bound to a Two-domain Fragment of Its Cellular Attachment Protein Decay-accelerating Factor (CD 55)^*

David Bhella, Ian G. Goodfellow¶||, Pietro Roversi**, David Pettigrew**, Yasmin Chaudhry¶¶¶, David J. Evans¶, and Susan M. Lea**

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

Echovirus type 12 (EV12), an Enterovirus of the Picornaviridae family, uses the complement regulator decay-accelerating factor (DAF, CD55) as a cellular receptor. We have calculated a three-dimensional reconstruction of EV12 bound to a fragment of DAF consisting of short consensus repeat domains 3 and 4 from cryo-negative stain electron microscopy data (EMD code 1057). This shows that, as for an earlier reconstruction of the related echovirus type 7 bound to DAF, attachment is not within the viral canyon but occurs close to the 2-fold symmetry axes. Despite this general similarity our reconstruction reveals a receptor interaction that is quite different from that observed for EV7. Fitting of the crystallographic co-ordinates for DAF₃₄ and EV11 into the reconstruction shows a close agreement between the crystal structure of the receptor fragment and the density for the virus-bound receptor, allowing unambiguous positioning of the receptor with respect to the virion (PDB code 1UPN). Our finding that the mode of virus-receptor interaction in EV12 is distinct from that seen for EV7 raises interesting questions regarding the evolution and biological significance of the DAF binding phenotype in these viruses.

Received for publication, October 15, 2003 , and in revised form, November 19, 2003.

^* 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.

^|| Current address: School of Animal and Microbial Sciences, University of Reading, P. O. Box 228, Reading, Berkshire RG6 6AJ, UK. Funded by Medical Research Council Program Grant G9901250 (to D. J. E.).

Funded by Biotechnology and Biological Sciences Research Council Grant 43/B16601 (to S. M. L.).

Funded by a Medical Research Council studentship award (to S. M. L.).

^¶¶ Current address: School of Animal and Microbial Sciences, University of Reading, P. O. Box 228, Reading, Berkshire RG6 6AJ, UK. Funded by Wellcome trust project Grant 059011 (to D. J. E.).

Supported by the United Kingdom Medical Research Council. To whom correspondence should be addressed. Tel.: 44-141-330-2988; E-mail: d.bhella{at}vir.gla.ac.uk.

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