Abstract
Rubella virus (RV) contains four structural proteins, C (capsid), E2a, E2b, and E1, which are derived from posttranslational processing of a single polyprotein precursor, p110. C protein is nonglycosylated and is thought to interact with RV RNA to form a nucleocapsid. E1 and E2 are membrane glycoproteins that form the spike complexes located on the virion exterior. Two different E1 cDNAs were used to analyze the requirements for translocation of E1 into the endoplasmic reticulum. Analysis of expression of these cDNAs both in vivo and in vitro showed that RV E1 was stably expressed and glycosylated in COS cells and correctly targeted into microsomes in the absence of E2 glycoprotein. The results provide experimental evidence that translocation of RV E1 glycoprotein into the endoplasmic reticulum is mediated by a signal peptide contained within the 69 carboxyl-terminal residues of E2.
MeSH Terms
Amino Acid Sequence
Base Sequence
Biological Transport
Blotting, Northern
Cell-Free System
Cells, Cultured
Cloning, Molecular
Endonucleases
Endoplasmic Reticulum/metabolism
Genes, Viral
Membrane Glycoproteins/metabolism
Microsomes/metabolism
Molecular Sequence Data
Mutation
Plasmids
Precipitin Tests
Protein Biosynthesis
Protein Sorting Signals/genetics,physiology
Restriction Mapping
Rubella virus/physiology
Single-Strand Specific DNA and RNA Endonucleases
Transfection
Viral Envelope Proteins/biosynthesis,physiology
Viral Proteins/metabolism
Viral Structural Proteins
Virus Replication
Chemicals
Membrane Glycoproteins
Protein Sorting Signals
Viral Envelope Proteins
Viral Proteins
Viral Structural Proteins
Endonucleases
Single-Strand Specific DNA and RNA Endonucleases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hobman T C
Department of Pathology, Faculty of Medicine, University of British Columbia, Vancouver, Canada.
Shukin R
Gillam S
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