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 Wang, S.
Right arrow Articles by Anderson, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wang, S.
Right arrow Articles by Anderson, R.

 Previous Article  |  Next Article 

Journal of Virology, March 1999, p. 2547-2551, Vol. 73, No. 3
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

PrM- and Cell-Binding Domains of the Dengue Virus E Protein

Songli Wang, Runtao He,dagger and Robert Anderson*

Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada

Received 25 August 1998/Accepted 30 November 1998

The E-prM proteins of flaviviruses are unusual complexes which play important roles in virus assembly and fusion modulation and in potential immunity-inducing vaccines. Despite their importance, little is known about the biogenesis and structural organization of E-prM complexes. Pulse-chase radiolabeling of dengue virus-infected Vero cells demonstrated a rapid interassociation of E and prM proteins, and sucrose gradient sedimentation analysis suggested that E-prM complexes progressed from simple heteromers to more densely sedimenting structures indicating increased multimerization. E-prM heteromers of even higher complexity were observed in virus particles, suggesting an intracellular assembly process which results in the networking of E-prM subunits into a lattice-like structure found in virus particles. Trypsin cleavage of E-prM-containing virus particles resulted in the release of a soluble 45-kDa fragment of the E protein which retained cell-binding activity. The results suggest that E-prM interactions in dengue virus particles are largely mediated by domains in the carboxy-terminal anchoring domain of E, while cell-binding activity is retained in a trypsin-releasable ectodomain of the E protein.


* Corresponding author. Mailing address: Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada. Phone: (902) 494-1063. Fax: (902) 494-5125. E-mail: Anderson{at}Tupdean1.med.dal.ca.

dagger Present address: Laboratory of Ocular Therapeutics, National Eye Institute, National Institutes of Health, Bethesda, MD 20892.


Journal of Virology, March 1999, p. 2547-2551, Vol. 73, No. 3
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Zybert, I. A., van der Ende-Metselaar, H., Wilschut, J., Smit, J. M. (2008). Functional importance of dengue virus maturation: infectious properties of immature virions. J. Gen. Virol. 89: 3047-3051 [Abstract] [Full Text]  
  • Junjhon, J., Lausumpao, M., Supasa, S., Noisakran, S., Songjaeng, A., Saraithong, P., Chaichoun, K., Utaipat, U., Keelapang, P., Kanjanahaluethai, A., Puttikhunt, C., Kasinrerk, W., Malasit, P., Sittisombut, N. (2008). Differential Modulation of prM Cleavage, Extracellular Particle Distribution, and Virus Infectivity by Conserved Residues at Nonfurin Consensus Positions of the Dengue Virus pr-M Junction. J. Virol. 82: 10776-10791 [Abstract] [Full Text]  
  • Etemad, B., Batra, G., Raut, R., Dahiya, S., Khanam, S., Swaminathan, S., Khanna, N. (2008). An Envelope Domain III-based Chimeric Antigen Produced in Pichia pastoris Elicits Neutralizing Antibodies Against All Four Dengue Virus Serotypes. Am J Trop Med Hyg 79: 353-363 [Abstract] [Full Text]  
  • Kim, J.-M., Yun, S.-I., Song, B.-H., Hahn, Y.-S., Lee, C.-H., Oh, H.-W., Lee, Y.-M. (2008). A Single N-Linked Glycosylation Site in the Japanese Encephalitis Virus prM Protein Is Critical for Cell Type-Specific prM Protein Biogenesis, Virus Particle Release, and Pathogenicity in Mice. J. Virol. 82: 7846-7862 [Abstract] [Full Text]  
  • van der Schaar, H. M., Rust, M. J., Waarts, B.-L., van der Ende-Metselaar, H., Kuhn, R. J., Wilschut, J., Zhuang, X., Smit, J. M. (2007). Characterization of the Early Events in Dengue Virus Cell Entry by Biochemical Assays and Single-Virus Tracking. J. Virol. 81: 12019-12028 [Abstract] [Full Text]  
  • Brown, M. G., King, C. A., Sherren, C., Marshall, J. S., Anderson, R. (2006). A dominant role for Fc{gamma}RII in antibody-enhanced dengue virus infection of human mast cells and associated CCL5 release. J. Leukoc. Biol. 80: 1242-1250 [Abstract] [Full Text]  
  • Dinglasan, R. R., Jacobs-Lorena, M. (2005). Insight into a Conserved Lifestyle: Protein-Carbohydrate Adhesion Strategies of Vector-Borne Pathogens. Infect. Immun. 73: 7797-7807 [Full Text]  
  • Lin, Y.-J., Wu, S.-C. (2005). Histidine at Residue 99 and the Transmembrane Region of the Precursor Membrane prM Protein Are Important for the prM-E Heterodimeric Complex Formation of Japanese Encephalitis Virus. J. Virol. 79: 8535-8544 [Abstract] [Full Text]  
  • Pryor, M. J., Azzola, L., Wright, P. J., Davidson, A. D. (2004). Histidine 39 in the dengue virus type 2 M protein has an important role in virus assembly. J. Gen. Virol. 85: 3627-3636 [Abstract] [Full Text]  
  • Keelapang, P., Sriburi, R., Supasa, S., Panyadee, N., Songjaeng, A., Jairungsri, A., Puttikhunt, C., Kasinrerk, W., Malasit, P., Sittisombut, N. (2004). Alterations of pr-M Cleavage and Virus Export in pr-M Junction Chimeric Dengue Viruses. J. Virol. 78: 2367-2381 [Abstract] [Full Text]  
  • Allison, S. L., Tao, Y. J., O'Riordain, G., Mandl, C. W., Harrison, S. C., Heinz, F. X. (2003). Two Distinct Size Classes of Immature and Mature Subviral Particles from Tick-Borne Encephalitis Virus. J. Virol. 77: 11357-11366 [Abstract] [Full Text]  
  • Gritsun, T. S., Frolova, T. V., Zhankov, A. I., Armesto, M., Turner, S. L., Frolova, M. P., Pogodina, V. V., Lashkevich, V. A., Gould, E. A. (2002). Characterization of a Siberian Virus Isolated from a Patient with Progressive Chronic Tick-Borne Encephalitis. J. Virol. 77: 25-36 [Abstract] [Full Text]  
  • Twiddy, S. S., Woelk, C. H., Holmes, E. C. (2002). Phylogenetic evidence for adaptive evolution of dengue viruses in nature. J. Gen. Virol. 83: 1679-1689 [Abstract] [Full Text]  
  • Lorenz, I. C., Allison, S. L., Heinz, F. X., Helenius, A. (2002). Folding and Dimerization of Tick-Borne Encephalitis Virus Envelope Proteins prM and E in the Endoplasmic Reticulum. J. Virol. 76: 5480-5491 [Abstract] [Full Text]  
  • Mackenzie, J. M., Westaway, E. G. (2001). Assembly and Maturation of the Flavivirus Kunjin Virus Appear To Occur in the Rough Endoplasmic Reticulum and along the Secretory Pathway, Respectively. J. Virol. 75: 10787-10799 [Abstract] [Full Text]  
  • Courageot, M.-P., Frenkiel, M.-P., Duarte Dos Santos, C., Deubel, V., Desprès, P. (2000). alpha -Glucosidase Inhibitors Reduce Dengue Virus Production by Affecting the Initial Steps of Virion Morphogenesis in the Endoplasmic Reticulum. J. Virol. 74: 564-572 [Abstract] [Full Text]