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Journal of Virology, December 2003, p. 12710-12719, Vol. 77, No. 23
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.23.12710-12719.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Deletions in the Transmembrane Domain of a Sindbis Virus Glycoprotein Alter Virus Infectivity, Stability, and Host Range

Raquel Hernandez, Christine Sinodis, Michelle Horton, Davis Ferreira, Chunning Yang, and Dennis T. Brown*

Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh North Carolina 27695

Received 17 June 2003/ Accepted 18 August 2003

The alphaviruses are composed of two icosahedral protein shells, one nested within the other. A membrane bilayer derived from the host cell is sandwiched between the protein shells. The protein shells are attached to one another by protein domains which extend one of the proteins of the outer shell through the membrane bilayer to attach to the inner shell. We have examined the interaction of the membrane-spanning domain of one of the membrane glycoproteins with the membrane bilayer and with other virus proteins in an attempt to understand the role this domain plays in virus assembly and function. Through incremental deletions, we have reduced the length of a virus membrane protein transmembrane domain from its normal 26 amino acids to 8 amino acids. We examined the effect of these deletions on the assembly and function of virus particles. We found that progressive truncations in the transmembrane domain profoundly affected production of infectious virus in a cyclic fashion. We also found that membrane composition effects protein-protein and protein-membrane interactions during virus assembly.

* Corresponding author. Mailing address: Campus Box 7622, North Carolina State University, Raleigh, NC 27695-7622. Phone: (919) 515 5765. Fax: (919) 515-2047. E-mail: dennis_brown{at}ncsu.edu.

Journal of Virology, December 2003, p. 12710-12719, Vol. 77, No. 23
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.23.12710-12719.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hernandez, R., Paredes, A., Brown, D. T. (2008). Sindbis Virus Conformational Changes Induced by a Neutralizing Anti-E1 Monoclonal Antibody. J. Virol. 82: 5750-5760 [Abstract] [Full Text]  
  • Whitehurst, C. B., Soderblom, E. J., West, M. L., Hernandez, R., Goshe, M. B., Brown, D. T. (2007). Location and Role of Free Cysteinyl Residues in the Sindbis Virus E1 and E2 Glycoproteins. J. Virol. 81: 6231-6240 [Abstract] [Full Text]  
  • West, J., Hernandez, R., Ferreira, D., Brown, D. T. (2006). Mutations in the Endodomain of Sindbis Virus Glycoprotein E2 Define Sequences Critical for Virus Assembly. J. Virol. 80: 4458-4468 [Abstract] [Full Text]  
  • West, J., Brown, D. T. (2006). Role of a conserved tripeptide in the endodomain of Sindbis virus glycoprotein E2 in virus assembly and function.. J. Gen. Virol. 87: 657-664 [Abstract] [Full Text]  
  • Hernandez, R., Ferreira, D., Sinodis, C., Litton, K., Brown, D. T. (2005). Single Amino Acid Insertions at the Junction of the Sindbis Virus E2 Transmembrane Domain and Endodomain Disrupt Virus Envelopment and Alter Infectivity. J. Virol. 79: 7682-7697 [Abstract] [Full Text]  


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