JVI Accepts, published online ahead of print on 4 November 2009

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J. Virol. doi:10.1128/JVI.01625-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Investigation of clade B New World arenavirus tropism using chimeric GP1 proteins.

Vanessa K. Martin, Magali E. Droniou-Bonzom, Therese Reignier, Jill E. Oldenburg, Alex U. Cox, and Paula M. Cannon^*

University of Southern California Keck School of Medicine, Los Angeles, California, USA

^* To whom correspondence should be addressed. Email: pcannon{at}usc.edu.

Clade B of the New World arenaviruses contains both pathogenic and non-pathogenic members, whose surface glycoproteins (GP) are characterized by different abilities to use the human transferrin receptor type 1 (hTfR1) protein as a receptor. Using closely related pairs of pathogenic and non-pathogenic viruses, we investigated the determinants of the GP1 subunit that confer these different characteristics. We identified a central region (residues 85-221) in the Guanarito virus GP1 that was sufficient to interact with hTfR1, with residues 159-221 being essential. The recently solved structure of part of the Machupo virus GP1 suggests an explanation for these requirements.