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Journal of Virology, October 2000, p. 9313-9316, Vol. 74, No. 19
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Sindbis Virus Glycoprotein E1 Is Divided into Two Discrete Domains at Amino Acid 129 by Disulfide Bridge Connections

Brett S. Phinney and Dennis T. Brown*

Department of Biochemistry, North Carolina State University, Raleigh, North Carolina 27695

Received 12 May 2000/Accepted 10 July 2000

The E1 membrane glycoprotein of Sindbis virus contains structural and functional domains, which are conformationally dependent on the presence of intramolecular disulfide bridges (B. A. Abell and D. T. Brown, J. Virol. 67:5496-5501, 1993; R. P. Anthony, A. M. Paredes, and D. T. Brown, Virology 190:330-336, 1992). We have examined the disulfide bonds in E1 and have determined that the E1 membrane glycoprotein contains two separate sets of interconnecting disulfide linkages, which divide the protein into two domains at amino acid 129. These separate sets of disulfides may stabilize and define the structural and functional regions of the E1 protein.

* Corresponding author. Mailing address: Department of Biochemistry, North Carolina State University, Campus Box 7622, Raleigh, NC 27695. Phone: (919) 515-5802. Fax: (919) 515-2047. E-mail: dennis_brown{at}ncsu.edu.

Journal of Virology, October 2000, p. 9313-9316, Vol. 74, No. 19
0022-538X/00/$04.00+0
Copyright © 2000, 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]  


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