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 Dumonceaux, J.
Right arrow Articles by Dragic, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dumonceaux, J.
Right arrow Articles by Dragic, T.

 Previous Article  |  Next Article 

Journal of Virology, December 2003, p. 13418-13424, Vol. 77, No. 24
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.24.13418-13424.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Expression of Unmodified Hepatitis C Virus Envelope Glycoprotein-Coding Sequences Leads to Cryptic Intron Excision and Cell Surface Expression of E1/E2 Heterodimers Comprising Full-Length and Partially Deleted E1

Julie Dumonceaux ,1,{dagger},{ddagger} Emmanuel G. Cormier,1,2,{dagger} Francis Kajumo,1,2 Gerald P. Donovan,2 Jayanta Roy-Chowdhury,1 Ira J. Fox,3 Jason P. Gardner,2 and Tatjana Dragic1*

Albert Einstein College of Medicine, Bronx, New York 10461,1 Progenics Pharmaceuticals, Inc., Tarrytown, New York 10591,2 Department of Surgery, Nebraska Medical Center, Omaha, Nebraska 981983

Received 22 July 2003/ Accepted 12 September 2003

Hepatitis C virus (HCV) is a positive-strand RNA virus that replicates exclusively in the cytoplasm of infected cells. The viral envelope glycoproteins, E1 and E2, appear to be retained in the endoplasmic reticulum, where viral budding is thought to occur. Surprisingly, we found that the expression system used to generate HCV envelope glycoproteins influences their subcellular localization and processing. These findings have important implications for optimizing novel HCV fusion and entry assays as well as for budding and virus particle formation.

* Corresponding author. Mailing address: Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Phone: (718) 430-3282. Fax: (718) 430-8711. E-mail: tdragic{at}aecom.yu.edu.

{dagger} J.D. and E.G.C. contributed equally to this work.

{ddagger} Present address: Généthon, Groupe Cellules Souches, 91002 Evry Cedex, France.

Journal of Virology, December 2003, p. 13418-13424, Vol. 77, No. 24
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.24.13418-13424.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kobayashi, M., Bennett, M. C., Bercot, T., Singh, I. R. (2006). Functional Analysis of Hepatitis C Virus Envelope Proteins, Using a Cell-Cell Fusion Assay. J. Virol. 80: 1817-1825 [Abstract] [Full Text]  
  • Sandrin, V., Cosset, F.-L. (2006). Intracellular Versus Cell Surface Assembly of Retroviral Pseudotypes Is Determined by the Cellular Localization of the Viral Glycoprotein, Its Capacity to Interact with Gag, and the Expression of the Nef Protein. J. Biol. Chem. 281: 528-542 [Abstract] [Full Text]  
  • Sandrin, V., Boulanger, P., Penin, F., Granier, C., Cosset, F.-L., Bartosch, B. (2005). Assembly of functional hepatitis C virus glycoproteins on infectious pseudoparticles occurs intracellularly and requires concomitant incorporation of E1 and E2 glycoproteins. J. Gen. Virol. 86: 3189-3199 [Abstract] [Full Text]  
  • Cormier, E. G., Durso, R. J., Tsamis, F., Boussemart, L., Manix, C., Olson, W. C., Gardner, J. P., Dragic, T. (2004). L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells by hepatitis C virus. Proc. Natl. Acad. Sci. USA 101: 14067-14072 [Abstract] [Full Text]  
  • Flint, M., Logvinoff, C., Rice, C. M., McKeating, J. A. (2004). Characterization of Infectious Retroviral Pseudotype Particles Bearing Hepatitis C Virus Glycoproteins. J. Virol. 78: 6875-6882 [Abstract] [Full Text]  
  • Nielsen, S. U., Bassendine, M. F., Burt, A. D., Bevitt, D. J., Toms, G. L. (2004). Characterization of the genome and structural proteins of hepatitis C virus resolved from infected human liver. J. Gen. Virol. 85: 1497-1507 [Abstract] [Full Text]  
  • Cormier, E. G., Tsamis, F., Kajumo, F., Durso, R. J., Gardner, J. P., Dragic, T. (2004). CD81 is an entry coreceptor for hepatitis C virus. Proc. Natl. Acad. Sci. USA 101: 7270-7274 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»