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Unusual Molecular Architecture of the Machupo Virus Attachment Glycoprotein

DOI: 10.1128/JVI.00761-09 DOI Help
PMID: 19494008 PMID Help

Authors: Thomas Bowden (Division of Structural Biology, University of Oxford) , Max Crispin (Division of Structural Biology, University of Oxford) , David J Harvey (Department of Biochemistry, University of Oxford) , Jonathan Grimes (Division of Structural Biology, University of Oxford) , Edith Jones (University of Oxford) , Dave Stuart (Diamond Light Source) , Stephen Graham (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Virology , VOL 83 (16) , PAGES 8259-8265

State: Published (Approved)
Published: January 2009

Abstract: 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/beta 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.

Journal Keywords: Unusual Molecular Architecture Of The Machupo Virus Attachment Glycoprotein

Subject Areas: Biology and Bio-materials


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