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Journal of Virology, February 2006, p. 1290-1301, Vol. 80, No. 3
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.3.1290-1301.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

West Nile Virus Discriminates between DC-SIGN and DC-SIGNR for Cellular Attachment and Infection

Carl W. Davis,1 Hai-Yen Nguyen,1 Sheri L. Hanna,1 Melissa D. Sánchez,1 Robert W. Doms,1 and Theodore C. Pierson2*

Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania,1 Laboratory of Viral Diseases, National Institutes of Health, Bethesda, Maryland2

Received 27 June 2005/ Accepted 3 November 2005

The C-type lectins DC-SIGN and DC-SIGNR bind mannose-rich glycans with high affinity. In vitro, cells expressing these attachment factors efficiently capture, and are infected by, a diverse array of appropriately glycosylated pathogens, including dengue virus. In this study, we investigated whether these lectins could enhance cellular infection by West Nile virus (WNV), a mosquito-borne flavivirus related to dengue virus. We discovered that DC-SIGNR promoted WNV infection much more efficiently than did DC-SIGN, particularly when the virus was grown in human cell types. The presence of a single N-linked glycosylation site on either the prM or E glycoprotein of WNV was sufficient to allow DC-SIGNR-mediated infection, demonstrating that uncleaved prM protein present on a flavivirus virion can influence viral tropism under certain circumstances. Preferential utilization of DC-SIGNR was a specific property conferred by the WNV envelope glycoproteins. Chimeras between DC-SIGN and DC-SIGNR demonstrated that the ability of DC-SIGNR to promote WNV infection maps to its carbohydrate recognition domain. WNV virions and subviral particles bound to DC-SIGNR with much greater affinity than DC-SIGN. We believe this is the first report of a pathogen interacting more efficiently with DC-SIGNR than with DC-SIGN. Our results should lead to the discovery of new mechanisms by which these well-studied lectins discriminate among ligands.

* Corresponding author. Mailing address: Laboratory of Viral Diseases, National Institutes of Health, 4 Center Drive, Building 4, Room 216, Bethesda, MD 20892. Phone: (301) 451-7977. Fax: (301) 451-7978. E-mail: piersontc{at}mail.nih.gov.

Journal of Virology, February 2006, p. 1290-1301, Vol. 80, No. 3
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.3.1290-1301.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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