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Published February 1983 | Published
Journal Article Open

Structural proteins of Western equine encephalitis virus: amino acid compositions and N-terminal sequences


The structural proteins of Western equine encephalitis virus, a member of the alphavirus group, have been characterized by the determination of their amino acid compositions and by N-terminal sequence analysis. More than 60 residues of the N-terminal sequences of each of the envelope glycoproteins have been determined. A comparison of these sequences with the previously determined sequences of two related alphaviruses. Sindbis virus and Semliki Forest virus, strongly supports the view that all three viruses have evolved from a common ancestor and provides information on the pattern of this evolution. The analysis of the capsid proteins of Western equine encephalitis virus shows that the nucleocapsid of this virus can accommodate a considerable degree of variability in its protein component and that at least some regions of alphavirus capsid proteins show more extensive differences between different viruses than do the envelope glycoproteins.

Additional Information

Copyright © 1983 by the American Society for Microbiology. Received 23 September 1982/Accepted 5 November 1982 We thank Chin Sook Kim for her expert technical assistance. This work was supported by Public Health Service grants GM 06965 and AI 10793 from the National Institutes of Health and grant PCM 80 22830 from the National Science Foundation.

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