HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 48, 37183-37194, December 1, 2006

This Article Full Text Full Text (PDF) All Versions of this Article: 281/48/37183    most recent M605429200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Davis, C. W. Articles by Pierson, T. C. Search for Related Content PubMed PubMed Citation Articles by Davis, C. W. Articles by Pierson, T. C. Social Bookmarking                      What's this?

The Location of Asparagine-linked Glycans on West Nile Virions Controls Their Interactions with CD209 (Dendritic Cell-specific ICAM-3 Grabbing Nonintegrin)^*

Carl W. Davis¹, Lisa M. Mattei, Hai-Yen Nguyen, Camilo Ansarah-Sobrinho, Robert W. Doms, and Theodore C. Pierson²

From the Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 and the Viral Pathogenesis Section, Laboratory of Viral Diseases, National Institutes of Health, Bethesda, Maryland 20892

Mammalian cell-derived West Nile virus preferentially infects cells expressing the C-type lectin CD209L (dendritic cellspecific ICAM-3 grabbing nonintegrin-related protein; liver- and lymph node-specific ICAM-3 grabbing nonintegrin) but not cells expressing CD209 (dendritic cell-specific ICAM-3 grabbing nonintegrin). In contrast, Dengue virus infection is enhanced in cells expressing either attachment factor. The West Nile virus envelope (E) protein contains a single N-linked glycosylation site at residue 154, whereas Dengue virus E contains sites at residues 153 and 67. We introduced a glycosylation site at position 67 into West Nile virus E. Reporter virus particles pseudotyped with this E protein infected cells using either CD209 or CD209L. We also introduced glycosylation sites at several novel positions. All sites allowed CD209L-mediated infection, but only a subset promoted CD209 use. As seen for other viruses, mannose-rich glycans on West Nile virus were required for its interactions with CD209. Surprisingly, however, mannose-rich glycans were not required for CD209L-mediated infection. Complex glycans, particularly N-acetylglucosamine-terminated structures, were able to mediate reporter virus particle interactions with CD209L. We propose that CD209L recognizes glycosylated flaviviruses with broad specificity, whereas CD209 is selective for flaviviruses bearing mannose-rich glycans. The location of the N-linked glycosylation sites on a virion determines the types of glycans incorporated, thus controlling viral tropism for CD209-expressing cells.

Received for publication, June 6, 2006 , and in revised form, September 20, 2006.

^* This work was supported in part by National Institutes of Health Grants AI 50469 and U54 AI 57168 and in part by the Intramural Research Program of the NIAID, National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by National Institutes of Health Grant T32 AI 07632.

² To whom correspondence should be addressed: Laboratory of Viral Diseases, National Institutes of Health, 4 Center Dr., Bldg. 4, Rm. 216, Bethesda, MD 20892. Tel.: 301-451-7977; Fax: 301-451-7978; E-mail: piersontc{at}mail.nih.gov.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				K.-F. Kong, K. Delroux, X. Wang, F. Qian, A. Arjona, S. E. Malawista, E. Fikrig, and R. R. Montgomery Dysregulation of TLR3 Impairs the Innate Immune Response to West Nile Virus in the Elderly J. Virol., August 1, 2008; 82(15): 7613 - 7623. [Abstract] [Full Text] [PDF]

				D. J. Vigerust, K. B. Ulett, K. L. Boyd, J. Madsen, S. Hawgood, and J. A. McCullers N-Linked Glycosylation Attenuates H3N2 Influenza Viruses J. Virol., August 15, 2007; 81(16): 8593 - 8600. [Abstract] [Full Text] [PDF]

				J. A. Mondotte, P.-Y. Lozach, A. Amara, and A. V. Gamarnik Essential Role of Dengue Virus Envelope Protein N Glycosylation at Asparagine-67 during Viral Propagation J. Virol., July 1, 2007; 81(13): 7136 - 7148. [Abstract] [Full Text] [PDF]