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. 1983 Feb;45(2):708–714. doi: 10.1128/jvi.45.2.708-714.1983

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

J R Bell, M W Bond, M W Hunkapiller, E G Strauss, J H Strauss, K Yamamoto, B Simizu
PMCID: PMC256466  PMID: 6834471

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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