Article
Function of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1.
Journal of virology - 1 Sept 1990
Lobigs M, Zhao H X, Garoff H
Abstract excerpt
The Semliki Forest virus spike glycoproteins E1 and p62 form a heterodimeric complex in the endoplasmic reticulum (ER) and are transported as such to the cell surface. In the mature virus particle, the heterodimeric association of E1 and E2 (the cleavage product of p62) is maintained, but as a more labile and acid-sensitive oligomer than the E1-p62 complex. The E3 peptide forms the N-terminal part of the p62...
Topics
- Animals
- Base Sequence
- Cell Line
- Cell Membrane
- Fluorescent Antibody Technique
- Genetic Complementation Test
- Kinetics
- Macromolecular Substances
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes