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Published July 25, 1983 | public
Journal Article

Sequence Analysis of Two Mutants of Sindbis Virus Defective in the Intracellular Transport of Their Glycoproteins


We have sequenced the complementary DNA corresponding to the genes encoding the viral glycoproteins of tslO and ts23, mutants of Sindbis virus defective in the intracellular transport of their glycoproteins, and of revertants of these mutants. These studies have been augmented by direct amino acid sequencing of the amino-terminal regions of the glycoproteins of several virus strains. By comparing the deduced amino acid sequence with that of Sindbis HR virus, the parental strain of these mutants, and with the sequence of the revertants, we found ts23 to have a double mutation in glycoprotein El, while tsl0 was a single mutant in the same glycoprotein. In each case reversion to temperature insensitivity occurred by changes at the same site as the mutation, in two cases restoring the original amino acid and in the third case substituting an homologous amino acid (arginine in place of lysine). The three mutations were far apart from each other in the protein, suggesting that the three-dimensional conformation is very important for the correct migration of the glycoproteins from the rough endoplasmic reticulum to the plasma membrane. The sequence data also reveal that a number of other changes have occurred in the various virus strains during mutagenesis or passage.

Additional Information

© 1983 Academic Press Inc. (London) Ltd. Received 21 February 1983, and in revised form 24 March 1983. We are grateful to C. Rice for helpful discussions and advice on the sequencing experiments and to E. Lazarides for assistance with the immunofluorescence experiments. This work was supported by grants AI10793 and GM06965 from the National Institutes of Health and by grant PCM8022830 from the National Science Foundation. C.A. was supported by a grant from the Universidad Nacional Autónoma de México.

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