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Journal of Virology, May 2002, p. 5140-5146, Vol. 76, No. 10
0022-538X/02/$04.00+0 DOI: 10.1128/JVI.76.10.5140-5146.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
New World Arenavirus Clade C, but Not Clade A and B Viruses, Utilizes
-Dystroglycan as Its Major Receptor
Christina F. Spiropoulou,1* Stefan Kunz,2 Pierre E. Rollin,1 Kevin P. Campbell,3 and Michael B. A. Oldstone2
Special Pathogens Branch, Division of Viral and Rickettsial Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30333,1
Division of Virology, Department of Neuropharmacology, The Scripps Research Institute, La Jolla, California 92037,2
Department of Physiology, Neurology, and Biophysics, Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 522423
Received 20 November 2001/
Accepted 12 February 2002
-Dystroglycan (
-DG) has been identified as a major receptor for lymphocytic choriomeningitis virus (LCMV) and Lassa virus, two Old World arenaviruses. The situation with New World arenaviruses is less clear: previous studies demonstrated that Oliveros virus also exhibited high-affinity binding to
-DG but that Guanarito virus did not. To extend these initial studies, several additional Old and New World arenaviruses were screened for entry into mouse embryonic stem cells possessing or lacking
-DG. In addition, representative viruses were further analyzed for direct binding to
-DG by means of a virus overlay protein blot assay technique. These studies indicate that Old World arenaviruses use
-DG as a major receptor, whereas, of the New World arenaviruses, only clade C viruses (i.e., Oliveros and Latino viruses) use
-DG as a major receptor. New World clade A and B arenaviruses, which include the highly pathogenic Machupo, Guanarito, Junin, and Sabia viruses, appear to use a different receptor or coreceptor for binding. Previous studies with LCMV have suggested the need for a small aliphatic amino acid at LCMV GP1 glycoprotein amino acid position 260 to allow high-affinity binding to
-DG. As reported herein, this requirement appears to be broadly applicable to the arenaviruses as determined by more extensive analysis of
-DG receptor usage and GP1 sequences of Old and New World arenaviruses. In addition, GP1 amino acid position 259 also appears to be important, since all arenaviruses showing high-affinity
-DG binding possess a bulky aromatic amino acid (tyrosine or phenylalanine) at this position.
* Corresponding author. Mailing address: Special Pathogens Branch, Division of Viral and Rickettsial Diseases, Centers for Disease Control and Prevention, 1600 Clifton Rd., Atlanta, GA 30333. Phone: (404) 639-1115. Fax: (404) 693-1118. E-mail: ccs8{at}cdc.gov.
Journal of Virology, May 2002, p. 5140-5146, Vol. 76, No. 10
0022-538X/02/$04.00+0 DOI: 10.1128/JVI.76.10.5140-5146.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
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Copyright © 2002 by the American Society for Microbiology. All rights reserved.