This Article
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 Cartier, C.
Right arrow Articles by Boyer, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cartier, C.
Right arrow Articles by Boyer, V.

 Previous Article  |  Next Article 

J. Virol., Jun 1997, 4832-4837, Vol 71, No. 6
Copyright © 1997, American Society for Microbiology

Association of ERK2 mitogen-activated protein kinase with human immunodeficiency virus particles

C Cartier, M Deckert, C Grangeasse, R Trauger, F Jensen, A Bernard, A Cozzone, C Desgranges and V Boyer
INSERM U271, Lyon, France.

Here we report the presence of a protein kinase activity associated with human immunodeficiency virus type 1 (HIV-1) particles. We observed phosphorylation of five major proteins by the endogenous protein kinase activity. Phosphoamino acid analysis revealed phosphorylated serine and threonine residues. In addition, we observed autophosphorylation of two proteins in the presence of gamma-ATP in an in-gel phosphorylation assay. These two proteins are not linked by a disulfide bond, suggesting that two different protein kinases are associated with HIV-1 virions. Our results indicate the presence of ERK2 mitogen-activated protein kinase and of a 53,000-molecular-weight protein kinase associated with virions. Moreover, the use of different HIV strains derived from T cells and promonocytic cells, as well as the use of human T-cell leukemia virus type 1 particles, demonstrates that ERK2 is strongly associated with retrovirus particles in a cell-independent manner. Exogenous substrates, such as histone proteins, and a viral substrate, such as Gag protein, are phosphorylated by virus-associated protein kinases.


This article has been cited by other articles:

  • Leisenfelder, S. A., Kinchington, P. R., Moffat, J. F. (2008). Cyclin-Dependent Kinase 1/Cyclin B1 Phosphorylates Varicella-Zoster Virus IE62 and Is Incorporated into Virions. J. Virol. 82: 12116-12125 [Abstract] [Full Text]  
  • Law, L. J., Ilkow, C. S., Tzeng, W.-P., Rawluk, M., Stuart, D. T., Frey, T. K., Hobman, T. C. (2006). Analyses of Phosphorylation Events in the Rubella Virus Capsid Protein: Role in Early Replication Events. J. Virol. 80: 6917-6925 [Abstract] [Full Text]  
  • Cantin, R., Methot, S., Tremblay, M. J. (2005). Plunder and Stowaways: Incorporation of Cellular Proteins by Enveloped Viruses. J. Virol. 79: 6577-6587 [Full Text]  
  • Gurer, C., Hoglund, A., Hoglund, S., Luban, J. (2005). ATP{gamma}S Disrupts Human Immunodeficiency Virus Type 1 Virion Core Integrity. J. Virol. 79: 5557-5567 [Abstract] [Full Text]  
  • Rue, S. M., Roos, J. W., Tarwater, P. M., Clements, J. E., Barber, S. A. (2005). Phosphorylation and Proteolytic Cleavage of Gag Proteins in Budded Simian Immunodeficiency Virus. J. Virol. 79: 2484-2492 [Abstract] [Full Text]  
  • Lee, E. S., Kalantari, P., Tsutsui{section}, S., Klatt, A., Holden, J., Correll, P. H., Power{section}, C., Henderson, A. J. (2004). RON Receptor Tyrosine Kinase, a Negative Regulator of Inflammation, Inhibits HIV-1 Transcription in Monocytes/Macrophages and Is Decreased in Brain Tissue from Patients with AIDS. J. Immunol. 173: 6864-6872 [Abstract] [Full Text]  
  • Bennett, E. M., Lever, A. M. L., Allen, J. F. (2004). Human Immunodeficiency Virus Type 2 Gag Interacts Specifically with PRP4, a Serine-Threonine Kinase, and Inhibits Phosphorylation of Splicing Factor SF2. J. Virol. 78: 11303-11312 [Abstract] [Full Text]  
  • Hemonnot, B., Cartier, C., Gay, B., Rebuffat, S., Bardy, M., Devaux, C., Boyer, V., Briant, L. (2004). The Host Cell MAP Kinase ERK-2 Regulates Viral Assembly and Release by Phosphorylating the p6gag Protein of HIV-1. J. Biol. Chem. 279: 32426-32434 [Abstract] [Full Text]  
  • Owens, C. M., Song, B., Perron, M. J., Yang, P. C., Stremlau, M., Sodroski, J. (2004). Binding and Susceptibility to Postentry Restriction Factors in Monkey Cells Are Specified by Distinct Regions of the Human Immunodeficiency Virus Type 1 Capsid. J. Virol. 78: 5423-5437 [Abstract] [Full Text]  
  • Mansharamani, M., Graham, D. R. M., Monie, D., Lee, K. K., Hildreth, J. E. K., Siliciano, R. F., Wilson, K. L. (2003). Barrier-to-Autointegration Factor BAF Binds p55 Gag and Matrix and Is a Host Component of Human Immunodeficiency Virus Type 1 Virions. J. Virol. 77: 13084-13092 [Abstract] [Full Text]  
  • Cartier, C., Hemonnot, B., Gay, B., Bardy, M., Sanchiz, C., Devaux, C., Briant, L. (2003). Active cAMP-dependent Protein Kinase Incorporated within Highly Purified HIV-1 Particles Is Required for Viral Infectivity and Interacts with Viral Capsid Protein. J. Biol. Chem. 278: 35211-35219 [Abstract] [Full Text]  
  • Gaddis, N. C., Chertova, E., Sheehy, A. M., Henderson, L. E., Malim, M. H. (2003). Comprehensive Investigation of the Molecular Defect in vif-Deficient Human Immunodeficiency Virus Type 1 Virions. J. Virol. 77: 5810-5820 [Abstract] [Full Text]  
  • Muller, B., Patschinsky, T., Krausslich, H.-G. (2002). The Late-Domain-Containing Protein p6 Is the Predominant Phosphoprotein of Human Immunodeficiency Virus Type 1 Particles. J. Virol. 76: 1015-1024 [Abstract] [Full Text]  
  • Mu, J.-J., Chen, D.-S., Chen, P.-J. (2001). The Conserved Serine 177 in the Delta Antigen of Hepatitis Delta Virus Is One Putative Phosphorylation Site and Is Required for Efficient Viral RNA Replication. J. Virol. 75: 9087-9095 [Abstract] [Full Text]  
  • Planz, O., Pleschka, S., Ludwig, S. (2001). MEK-Specific Inhibitor U0126 Blocks Spread of Borna Disease Virus in Cultured Cells. J. Virol. 75: 4871-4877 [Abstract] [Full Text]  
  • Yang, X., Chen, Y., Gabuzda, D. (1999). ERK MAP Kinase Links Cytokine Signals to Activation of Latent HIV-1 Infection by Stimulating a Cooperative Interaction of AP-1 and NF-kappa B. J. Biol. Chem. 274: 27981-27988 [Abstract] [Full Text]  
  • Cartier, C., Sivard, P., Tranchat, C., Decimo, D., Desgranges, C., Boyer, V. (1999). Identification of Three Major Phosphorylation Sites within HIV-1 Capsid. ROLE OF PHOSPHORYLATION DURING THE EARLY STEPS OF INFECTION. J. Biol. Chem. 274: 19434-19440 [Abstract] [Full Text]  
  • Yang, X., Gabuzda, D. (1999). Regulation of Human Immunodeficiency Virus Type 1 Infectivity by the ERK Mitogen-Activated Protein Kinase Signaling Pathway. J. Virol. 73: 3460-3466 [Abstract] [Full Text]  
  • Ulich, C., Dunne, A., Parry, E., Hooker, C. W., Gaynor, R. B., Harrich, D. (1999). Functional Domains of Tat Required for Efficient Human Immunodeficiency Virus Type 1 Reverse Transcription. J. Virol. 73: 2499-2508 [Abstract] [Full Text]  
  • Yang, X., Gabuzda, D. (1998). Mitogen-activated Protein Kinase Phosphorylates and Regulates the HIV-1 Vif Protein. J. Biol. Chem. 273: 29879-29887 [Abstract] [Full Text]  
  • Emerman, M., Malim, M. H. (1998). HIV-1 Regulatory/Accessory Genes: Keys to Unraveling Viral and Host Cell Biology. Science 280: 1880-1884 [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»