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 Odell, D.
Right arrow Articles by Ghosh, H. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Odell, D.
Right arrow Articles by Ghosh, H. P.

 Previous Article  |  Next Article 

J. Virol., Oct 1997, 7996-8000, Vol 71, No. 10
Copyright © 1997, American Society for Microbiology

Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G

D Odell, E Wanas, J Yan and HP Ghosh
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.

Chimeric proteins in which the transmembrane anchoring sequence (TM) or both the TM and the cytoplasmic tail (CT) of vesicular stomatitis virus glycoprotein G were replaced with corresponding domains of viral or cellular integral membrane proteins were used to examine the influence of these domains on acidic-pH-induced membrane fusion by G protein. The TM and CT of G were also replaced with the lipid anchor glycosylphosphatidylinositol. Hybrids containing foreign TM or TM and CT sequences were fusogenic at acidic pH but glycosylphosphatidylinositol-anchored G was nonfusogenic at acidic pH. The results suggest that the fusogenic activity of G protein requires membrane anchoring by a hydrophobic peptide sequence and the specific amino acid sequence of the TM has no influence on fusogenic activity.


This article has been cited by other articles:

  • Barry, C., Duncan, R. (2009). Multifaceted Sequence-Dependent and -Independent Roles for Reovirus FAST Protein Cytoplasmic Tails in Fusion Pore Formation and Syncytiogenesis. J. Virol. 83: 12185-12195 [Abstract] [Full Text]  
  • Clancy, E. K., Duncan, R. (2009). Reovirus FAST Protein Transmembrane Domains Function in a Modular, Primary Sequence-Independent Manner To Mediate Cell-Cell Membrane Fusion. J. Virol. 83: 2941-2950 [Abstract] [Full Text]  
  • Li, Z., Blissard, G. W. (2008). Functional Analysis of the Transmembrane (TM) Domain of the Autographa californica Multicapsid Nucleopolyhedrovirus GP64 Protein: Substitution of Heterologous TM Domains. J. Virol. 82: 3329-3341 [Abstract] [Full Text]  
  • Ciczora, Y., Callens, N., Penin, F., Pecheur, E.-I., Dubuisson, J. (2007). Transmembrane Domains of Hepatitis C Virus Envelope Glycoproteins: Residues Involved in E1E2 Heterodimerization and Involvement of These Domains in Virus Entry. J. Virol. 81: 2372-2381 [Abstract] [Full Text]  
  • Ungermann, C., Langosch, D. (2005). Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing. J. Cell Sci. 118: 3819-3828 [Abstract] [Full Text]  
  • Miyauchi, K., Komano, J., Yokomaku, Y., Sugiura, W., Yamamoto, N., Matsuda, Z. (2005). Role of the Specific Amino Acid Sequence of the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 in Membrane Fusion. J. Virol. 79: 4720-4729 [Abstract] [Full Text]  
  • Rocha, A., Ruiz, S., Tafalla, C., Coll, J. M. (2004). Conformation- and Fusion-Defective Mutations in the Hypothetical Phospholipid-Binding and Fusion Peptides of Viral Hemorrhagic Septicemia Salmonid Rhabdovirus Protein G. J. Virol. 78: 9115-9122 [Abstract] [Full Text]  
  • Basu, A., Beyene, A., Meyer, K., Ray, R. (2004). The Hypervariable Region 1 of the E2 Glycoprotein of Hepatitis C Virus Binds to Glycosaminoglycans, but This Binding Does Not Lead to Infection in a Pseudotype System. J. Virol. 78: 4478-4486 [Abstract] [Full Text]  
  • Jeetendra, E., Ghosh, K., Odell, D., Li, J., Ghosh, H. P., Whitt, M. A. (2003). The Membrane-Proximal Region of Vesicular Stomatitis Virus Glycoprotein G Ectodomain Is Critical for Fusion and Virus Infectivity. J. Virol. 77: 12807-12818 [Abstract] [Full Text]  
  • Shmulevitz, M., Salsman, J., Duncan, R. (2003). Palmitoylation, Membrane-Proximal Basic Residues, and Transmembrane Glycine Residues in the Reovirus p10 Protein Are Essential for Syncytium Formation. J. Virol. 77: 9769-9779 [Abstract] [Full Text]  
  • Harman, A., Browne, H., Minson, T. (2002). The Transmembrane Domain and Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein H Play a Role in Membrane Fusion. J. Virol. 76: 10708-10716 [Abstract] [Full Text]  
  • Maillard, A. P., Gaudin, Y. (2002). Rabies virus glycoprotein can fold in two alternative, antigenically distinct conformations depending on membrane-anchor type. J. Gen. Virol. 83: 1465-1476 [Abstract] [Full Text]  
  • Estepa, A. M., Rocha, A. I., Mas, V., Perez, L., Encinar, J. A., Nunez, E., Fernandez, A., Gonzalez Ros, J. M., Gavilanes, F., Coll, J. M. (2001). A Protein G Fragment from the Salmonid Viral Hemorrhagic Septicemia Rhabdovirus Induces Cell-to-Cell Fusion and Membrane Phosphatidylserine Translocation at Low pH. J. Biol. Chem. 276: 46268-46275 [Abstract] [Full Text]  
  • West, J. T., Johnston, P. B., Dubay, S. R., Hunter, E. (2001). Mutations within the Putative Membrane-Spanning Domain of the Simian Immunodeficiency Virus Transmembrane Glycoprotein Define the Minimal Requirements for Fusion, Incorporation, and Infectivity. J. Virol. 75: 9601-9612 [Abstract] [Full Text]  
  • Kozerski, C., Ponimaskin, E., Schroth-Diez, B., Schmidt, M. F. G., Herrmann, A. (2000). Modification of the Cytoplasmic Domain of Influenza Virus Hemagglutinin Affects Enlargement of the Fusion Pore. J. Virol. 74: 7529-7537 [Abstract] [Full Text]  
  • Markosyan, R. M., Cohen, F. S., Melikyan, G. B. (2000). The Lipid-anchored Ectodomain of Influenza Virus Hemagglutinin (GPI-HA) Is Capable of Inducing Nonenlarging Fusion Pores. Mol. Biol. Cell 11: 1143-1152 [Abstract] [Full Text]  
  • Anderson, D. B., Laquerre, S., Goins, W. F., Cohen, J. B., Glorioso, J. C. (2000). Pseudotyping of Glycoprotein D-Deficient Herpes Simplex Virus Type 1 with Vesicular Stomatitis Virus Glycoprotein G Enables Mutant Virus Attachment and Entry. J. Virol. 74: 2481-2487 [Abstract] [Full Text]  
  • Roberts, P. C., Kipperman, T., Compans, R. W. (1999). Vesicular Stomatitis Virus G Protein Acquires pH-Independent Fusion Activity during Transport in a Polarized Endometrial Cell Line. J. Virol. 73: 10447-10457 [Abstract] [Full Text]  
  • Taylor, G. M., Sanders, D. A. (1999). The Role of the Membrane-spanning Domain Sequence in Glycoprotein-mediated Membrane Fusion. Mol. Biol. Cell 10: 2803-2815 [Abstract] [Full Text]  
  • Melikyan, G. B., Lin, S., Roth, M. G., Cohen, F. S. (1999). Amino Acid Sequence Requirements of the Transmembrane and Cytoplasmic Domains of Influenza Virus Hemagglutinin for Viable Membrane Fusion. Mol. Biol. Cell 10: 1821-1836 [Abstract] [Full Text]  
  • Pietschmann, T., Heinkelein, M., Heldmann, M., Zentgraf, H., Rethwilm, A., Lindemann, D. (1999). Foamy Virus Capsids Require the Cognate Envelope Protein for Particle Export. J. Virol. 73: 2613-2621 [Abstract] [Full Text]  
  • Cleverley, D. Z., Lenard, J. (1998). The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G protein. Proc. Natl. Acad. Sci. USA 95: 3425-3430 [Abstract] [Full Text]  
  • Carneiro, F. A., Ferradosa, A. S., Da Poian, A. T. (2001). Low pH-induced Conformational Changes in Vesicular Stomatitis Virus Glycoprotein Involve Dramatic Structure Reorganization. J. Biol. Chem. 276: 62-67 [Abstract] [Full Text]  
  • Langosch, D., Brosig, B., Pipkorn, R. (2001). Peptide Mimics of the Vesicular Stomatitis Virus G-protein Transmembrane Segment Drive Membrane Fusion in Vitro. J. Biol. Chem. 276: 32016-32021 [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»