Rubella E1
Protein is >90% pure as determined by SDS-PAGE.
Description
Product Specs
Product Science Overview
Rubella virus (RuV) is an enveloped, positive-sense RNA virus belonging to the Rubivirus genus. It is the causative agent of rubella, also known as German measles, a contagious disease that can lead to severe birth defects if contracted by pregnant women. The E1 glycoprotein of RuV plays a crucial role in the virus’s ability to infect host cells and is a key target for vaccine development.
The preparation of Rubella Virus E1 Mosaic Recombinant involves the use of recombinant DNA technology. This process typically includes:
- Cloning: The gene encoding the E1 glycoprotein is cloned into an expression vector.
- Expression: The recombinant vector is introduced into a suitable host cell line, such as E. coli or mammalian cells, to express the E1 protein.
- Purification: The expressed E1 protein is then purified using techniques such as affinity chromatography.
- Characterization: The purified protein is characterized to confirm its identity and functionality.
The E1 glycoprotein is an integral membrane protein that mediates the fusion of the viral envelope with the host cell membrane, facilitating viral entry. It is also involved in the assembly and release of new viral particles. The E1 protein contains several epitopes that are recognized by the immune system, making it a critical component of the immune response to RuV infection.
The primary function of the E1 glycoprotein is to facilitate the entry of the rubella virus into host cells. It does this by binding to specific receptors on the surface of the host cell and mediating the fusion of the viral envelope with the host cell membrane. This fusion process is pH-dependent and occurs in the acidic environment of the endosome.
The E1 glycoprotein undergoes conformational changes in response to the acidic pH of the endosome, which triggers the fusion of the viral envelope with the endosomal membrane. This fusion event releases the viral RNA into the host cell cytoplasm, where it can be translated and replicated to produce new viral particles.
The expression and function of the E1 glycoprotein are tightly regulated by both viral and host factors. Post-translational modifications, such as glycosylation, play a significant role in the proper folding and functionality of the E1 protein. Additionally, the interaction of E1 with other viral proteins, such as the E2 glycoprotein, is essential for the assembly and release of infectious viral particles.
