Published June 1982
| public
Journal Article
The N-Terminus of PE2 in Sindbis Virus-Infected Cells
Abstract
One of the two envelope glycoproteins of Sindbis virus, E2, and its intracellular precursor PE2 were obtained in chemically pure form from Sindbis infected cells by immunoabsorption with antibody against E2. The N-terminus of PE2, which is probably the signal sequence of this protein, was examined and two N-termini were found. One, the primary product of translation, was sequenced by Edman degradation and the other was found to be blocked and produced by N-acetylation of the first. It was also found that an asparagine residue at position 14 of PE2 is glycosylated. The putative signal sequence is not cleaved by signal peptidase either under normal conditions or when glycosylation is prevented with tunicamycin.
Additional Information
© 1982 by Academic Press, Inc. Received August 4, 1981; accepted February 11, 1982. We wish to thank L. E. Hood for this advice and assistance and E. Lenches for preparing the chick embryo fibroblasts. This investigation was supported by Grants GM06965 and AI10793 from the National Institutes of Health and by Grant PCM80-22830 from the National Science Foundation. J.R.B. was supported in part by training Grant GM00086 from the National Institutes of Health.Additional details
- Eprint ID
- 67137
- Resolver ID
- CaltechAUTHORS:20160516-151803038
- GM 06965
- NIH
- AI 10793
- NIH
- PCM 80-22830
- NSF
- GM-00086
- NIH Predoctoral Fellowship
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2016-05-17Created from EPrint's datestamp field
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