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 Husain, M.
Right arrow Articles by Moss, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Husain, M.
Right arrow Articles by Moss, B.

 Previous Article  |  Next Article 

Journal of Virology, November 2003, p. 11754-11766, Vol. 77, No. 21
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.21.11754-11766.2003

Evidence against an Essential Role of COPII-Mediated Cargo Transport to the Endoplasmic Reticulum-Golgi Intermediate Compartment in the Formation of the Primary Membrane of Vaccinia Virus

Matloob Husain and Bernard Moss*

Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0445

Received 5 June 2003/ Accepted 21 July 2003

Vaccinia virus assembles two distinct lipoprotein membranes. The primary membrane contains nonglycosylated proteins, appears as crescents in the cytoplasm, and delimits immature and mature intracellular virions. The secondary or wrapping membrane contains glycoproteins, is derived from virus-modified trans-Golgi or endosomal cisternae, forms a loose coat around some intracellular mature virions, and becomes the envelope of extracellular virions. Although the mode of formation of the wrapping membrane is partially understood, we know less about the primary membrane. Recent reports posit that the primary membrane originates from the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). According to this model, viral primary membrane proteins are cotranslationally inserted into the ER and accumulate in the ERGIC. To test the ERGIC model, we employed Sar1H79G, a dominant negative form of the Sar1 protein, which is an essential component of coatomer protein II (COPII)-mediated cargo transport from the ER to the ERGIC and other post-ER compartments. Overexpression of Sar1H79G by transfection or by a novel recombinant vaccinia virus with an inducible Sar1H79G gene resulted in retention of ERGIC 53 in the ER but did not interfere with localization of viral primary membrane proteins in factory regions or with formation of viral crescent membranes and infectious intracellular mature virions. Wrapping of intracellular mature virions and formation of extracellular virions did not occur, however, because some proteins that are essential for the secondary membrane were retained in the ER as a consequence of Sar1H79G overexpression. Our data argue against an essential role of COPII-mediated cargo transport and the ERGIC in the formation of the viral primary membrane. Instead, viral membranes may be derived directly from the ER or by a novel mechanism.

* Corresponding author. Mailing address: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 4 Center Dr., MSC 0445, NIH, Bethesda, MD 20892-0445. Phone: (301) 496-9869. Fax: (301) 480-1147. E-mail: bmoss{at}nih.gov.

Journal of Virology, November 2003, p. 11754-11766, Vol. 77, No. 21
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.21.11754-11766.2003




This article has been cited by other articles:

  • Zhang, L., Lee, S. Y., Beznoussenko, G. V., Peters, P. J., Yang, J.-S., Gilbert, H.-y., Brass, A. L., Elledge, S. J., Isaacs, S. N., Moss, B., Mironov, A., Hsu, V. W. (2009). A role for the host coatomer and KDEL receptor in early vaccinia biogenesis. Proc. Natl. Acad. Sci. USA 106: 163-168 [Abstract] [Full Text]  
  • Siddiqi, S. A., Mansbach, C. M. II (2008). PKC{zeta}-mediated phosphorylation controls budding of the pre-chylomicron transport vesicle. J. Cell Sci. 121: 2327-2338 [Abstract] [Full Text]  
  • Husain, M., Weisberg, A. S., Moss, B. (2007). Sequence-Independent Targeting of Transmembrane Proteins Synthesized within Vaccinia Virus Factories to Nascent Viral Membranes. J. Virol. 81: 2646-2655 [Abstract] [Full Text]  
  • Ju, H.-J., Brown, J. E., Ye, C.-M., Verchot-Lubicz, J. (2007). Mutations in the Central Domain of Potato Virus X TGBp2 Eliminate Granular Vesicles and Virus Cell-to-Cell Trafficking. J. Virol. 81: 1899-1911 [Abstract] [Full Text]  
  • Husain, M., Weisberg, A. S., Moss, B. (2006). Existence of an operative pathway from the endoplasmic reticulum to the immature poxvirus membrane. Proc. Natl. Acad. Sci. USA 103: 19506-19511 [Abstract] [Full Text]  
  • Siddiqi, S. A., Siddiqi, S., Mahan, J., Peggs, K., Gorelick, F. S., Mansbach, C. M. II (2006). The Identification of a Novel Endoplasmic Reticulum to Golgi SNARE Complex Used by the Prechylomicron Transport Vesicle. J. Biol. Chem. 281: 20974-20982 [Abstract] [Full Text]  
  • Heuser, J. (2005). Deep-etch EM reveals that the early poxvirus envelope is a single membrane bilayer stabilized by a geodetic "honeycomb" surface coat. JCB 169: 269-283 [Abstract] [Full Text]  
  • Husain, M., Moss, B. (2005). Role of Receptor-Mediated Endocytosis in the Formation of Vaccinia Virus Extracellular Enveloped Particles. J. Virol. 79: 4080-4089 [Abstract] [Full Text]  
  • Cyrklaff, M., Risco, C., Fernandez, J. J., Jimenez, M. V., Esteban, M., Baumeister, W., Carrascosa, J. L. (2005). Cryo-electron tomography of vaccinia virus. Proc. Natl. Acad. Sci. USA 102: 2772-2777 [Abstract] [Full Text]  
  • Punjabi, A., Traktman, P. (2005). Cell Biological and Functional Characterization of the Vaccinia Virus F10 Kinase: Implications for the Mechanism of Virion Morphogenesis. J. Virol. 79: 2171-2190 [Abstract] [Full Text]  
  • da Fonseca, F. G., Weisberg, A. S., Caeiro, M. F., Moss, B. (2004). Vaccinia Virus Mutants with Alanine Substitutions in the Conserved G5R Gene Fail To Initiate Morphogenesis at the Nonpermissive Temperature. J. Virol. 78: 10238-10248 [Abstract] [Full Text]  
  • Senkevich, T. G., Ward, B. M., Moss, B. (2004). Vaccinia Virus A28L Gene Encodes an Essential Protein Component of the Virion Membrane with Intramolecular Disulfide Bonds Formed by the Viral Cytoplasmic Redox Pathway. J. Virol. 78: 2348-2356 [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»