This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lin, G.
Right arrow Articles by Doms, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lin, G.
Right arrow Articles by Doms, R. W.

 Previous Article  |  Next Article 

Journal of Virology, January 2003, p. 1337-1346, Vol. 77, No. 2
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.2.1337-1346.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Differential N-Linked Glycosylation of Human Immunodeficiency Virus and Ebola Virus Envelope Glycoproteins Modulates Interactions with DC-SIGN and DC-SIGNR

George Lin,1 Graham Simmons,2 Stefan Pöhlmann,2 Frédéric Baribaud,2 Houping Ni,3 George J. Leslie,2 Beth S. Haggarty,1 Paul Bates,2 Drew Weissman,3 James A. Hoxie,1 and Robert W. Doms2*

Hematology-Oncology Division, Department of Medicine,1 Department of Microbiology,2 Division of Infectious Diseases, University of Pennsylvania, Philadelphia, Pennsylvania 191043

Received 8 July 2002/ Accepted 27 September 2002

The C-type lectins DC-SIGN and DC-SIGNR [collectively referred to as DC-SIGN(R)] bind and transmit human immunodeficiency virus (HIV) and simian immunodeficiency virus to T cells via the viral envelope glycoprotein (Env). Other viruses containing heavily glycosylated glycoproteins (GPs) fail to interact with DC-SIGN(R), suggesting some degree of specificity in this interaction. We show here that DC-SIGN(R) selectively interact with HIV Env and Ebola virus GPs containing more high-mannose than complex carbohydrate structures. Modulation of N-glycans on Env or GP through production of viruses in different primary cells or in the presence of the mannosidase I inhibitor deoxymannojirimycin dramatically affected DC-SIGN(R) infectivity enhancement. Further, murine leukemia virus, which typically does not interact efficiently with DC-SIGN(R), could do so when produced in the presence of deoxymannojirimycin. We predict that other viruses containing GPs with a large proportion of high-mannose N-glycans will efficiently interact with DC-SIGN(R), whereas those with solely complex N-glycans will not. Thus, the virus-producing cell type is an important factor in dictating both N-glycan status and virus interactions with DC-SIGN(R), which may impact virus tropism and transmissibility in vivo.


* Corresponding author. Mailing address: Department of Microbiology, University of Pennsylvania, 225 Johnson Pavilion, 3610 Hamilton Walk, Philadelphia, PA 19104. Phone: (215) 898-0890. Fax: (215) 898-9557. E-mail: doms{at}mail.med.upenn.edu.


Journal of Virology, January 2003, p. 1337-1346, Vol. 77, No. 2
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.2.1337-1346.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Pashov, A., Canziani, G., Monzavi-Karbassi, B., Kaveri, S. V., MacLeod, S., Saha, R., Perry, M., VanCott, T. C., Kieber-Emmons, T. (2005). Antigenic Properties of Peptide Mimotopes of HIV-1-associated Carbohydrate Antigens. J. Biol. Chem. 280: 28959-28965 [Abstract] [Full Text]