Recombinant RuV E1 protein (a.a. 157-276) [His]

Name: Recombinant RuV E1 protein (a.a. 157-276) [His]
SKU: DAG2000
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RuV E1 protein (aa 157 - 276) [His], recombinant protein from E. coli

COA

SDS

Datasheet

Summary

Product Overview

C-terminal 6xHis tagged E1 immunodominant region (a.a. 157-276)

Nature

Recombinant

Tag/Conjugate

His

Purity

≥ 90%

Format

Each vial contains 100 μg of lyophilized protein in 500mM NaCl, 50mM Phosphat buffer (pH 7.4), 200mM imidazole.

Concentration

1 mg/ml

Preservative

None

Storage

2-8°C short term, -20°C long term

Introduction

Rubella virus is the only member of the Rubrivirus genus of the Togavirus family. Unlike most Togaviruses it is NOT arthropod borne, but is acquired via the respiratory route. It causes German measles ( a mild contagious eruptive disease, capable of producing congenital defects in infants born to mothers infected during the first three months of pregnancy).

Antigen Description

The capsid protein (CP) has different functions. Its main tasks are the formation of homooligomeres to form the capsid, and the binding of the genomic RNA. Further is it responsible for the aggregation of RNA in the capsid, it interacts with the membrane proteins E1 and E2 and binds the human host-protein p32 which is important for replication of the virus in the host.As opposed to alpha viruses the capsid does not undergo autoprotolysis, rather is it cut off from the rest of the polyprotein by the signal-peptidase. Production of the capsid happens at the surface of intracellular membranes simultaneously with the budding of the virus.

Keywords

Coat protein; german measles; german measles capsid protein; p110; rubella capsid; Structural polyprotein; Rubella Virus Capsid; Togaviridae; Rubivirus

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Documents

pdf COA

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pdf Datasheet

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References

Recognition of contiguous allele-specific peptide elements in the Rubella virus E1 envelope protein

VACCINE

Authors: Nepom, GT; Domeier, ME; Ou, DW; Kovats, S; Mitchell, LA; Tingle, AJ

Abstract

Peptides which bind to human HLA-DRB1 class II molecules in an allele-specific fashion were derived from the immunodominant E1 envelope protein of rubella virus. Two nonoverlapping E1 peptide epitopes were recognized by rubella virus-specific T cells in the context of independent HLA alleles when presented either separately or as a contiguous polypeptide containing both epitopes. Direct binding analysis of potential peptide epitopes to distinct HLA molecules provides a direct approach for selecting antigenic peptides useful for epitope-based vaccine targeted to multiple HLA types. (C) 1997 Elsevier Science Ltd.

THE RUBELLA VIRUS-E1 GLYCOPROTEIN IS ARRESTED IN A NOVEL POST-ER, PRE-GOLGI COMPARTMENT

JOURNAL OF CELL BIOLOGY

Authors: HOBMAN, TC; WOODWARD, L; FARQUHAR, MG

Abstract

Evidence is accumulating that a distinct compartment(s) exists in the secretory pathway interposed between the rough ER (RER) and the Golgi stack. In this study we have defined a novel post-RER, pre-Golgi compartment where unassembled subunits of rubella virus (RV) E1 glycoprotein accumulate. When RV E1 is expressed in CHO cells in the absence of E2 glycoprotein, transport of E1 to the Golgi complex is arrested. The compartment in which E1 accumulates consists of a tubular network of smooth membranes which is in continuity with the RER but has distinctive properties from either the RER, Golgi, or previously characterized intermediate compartments. It lacks RER and Golgi membrane proteins and is not disrupted by agents which disrupt either the RER (thapsigargin, ionomycin) or Golgi (nocodazole and brefeldin A). However, luminal ER proteins bearing the KDEL signal have access to this compartment. Kinetically the site of E1 arrest lies distal to or at the site where palmitylation occurs and proximal to the low temperature 15-degrees-C block. Taken together the findings suggest that the site of E1 arrest corresponds to, or is located close to the exit site from the ER. This compartment could be identified morphologically because it is highly amplified in cells overexpressing unassembled E1 subunits, but it may have its counterpart among the transitional elements of non-transfected cells. We conclude that the site of E1 arrest may represent a new compartment or a differentiated proximal moiety of the intermediate compartment.