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Journal of Virology, August 2009, p. 8259-8265, Vol. 83, No. 16
0022-538X/09/$08.00+0     doi:10.1128/JVI.00761-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Unusual Molecular Architecture of the Machupo Virus Attachment Glycoprotein{triangledown} ,{dagger}

Thomas A. Bowden,1 Max Crispin,2 Stephen C. Graham,1 David J. Harvey,2 Jonathan M. Grimes,1 E. Yvonne Jones,1 and David I. Stuart1*

Division of Structural Biology, University of Oxford, Henry Wellcome Building of Genomic Medicine, Roosevelt Drive, Oxford OX3 7BN, United Kingdom,1 Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom2

Received 14 April 2009/ Accepted 26 May 2009

New World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor. This first structure of an arenavirus glycoprotein shows that GP1 consists of a novel {alpha}/β fold. This provides a blueprint of the New World arenavirus attachment glycoproteins and reveals a new architecture of viral attachment, using a protein fold of unknown origins.

* Corresponding author. Mailing address: Division of Structural Biology, University of Oxford, Henry Wellcome Building of Genomic Medicine, Roosevelt Drive, Oxford OX3 7BN, United Kingdom. Phone: 44 1865 287546. Fax: 44 1865 287547. E-mail: dave{at}strubi.ox.ac.uk

{triangledown} Published ahead of print on 3 June 2009.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, August 2009, p. 8259-8265, Vol. 83, No. 16
0022-538X/09/$08.00+0     doi:10.1128/JVI.00761-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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