Rubella virus cDNA and Antigen

Rubella, also known as German measles, is a contagious viral infection. It is caused by the rubella virus and is most common in children and young adults. Symptoms of rubella usually include a rash, swollen lymph nodes, and fever. In some cases, there may also be joint pain and redness of the eyes. Complications of rubella can include hearing loss, damage to the heart, and developmental delays in unborn babies if a woman becomes infected during pregnancy. Rubella can be prevented with the rubella vaccine.

Rubella virus antigen is a protein found on the surface of the rubella virus and is used to identify the virus. It is made up of two subunits, the E1 and E2 glycoproteins, which are responsible for binding to the host cell receptor and the virus’ entry into the cell. The antigen can be detected in the blood or other body fluids by serologic tests.

The rubella virus genome is composed of an approximately 6,000 nucleotide long, single-stranded, positive-sense RNA molecule. The genome contains six structural proteins: capsid (C), E1, E2, E3, and the putative proteins P and H. It also contains four nonstructural proteins: NS1, NS2, NS3, and NS4. The genome organization of the rubella virus is like that of other members of the family Togaviridae. The capsid (C) protein is located at the 5′ end of the genome, followed by the nonstructural proteins NS1, NS2, NS3 and NS4. The E1 and E3 proteins are located next, followed by the E2 and P proteins, and finally, the H protein is located at the 3′ end of the genome.

The genome of rubella virus is a single-stranded RNA molecule that is approximately 10,000 nucleotides long. The RNA encodes a single large polyprotein that is translated from the viral RNA genome. The polyprotein is then cleaved into individual functional proteins by viral proteases.

One of the proteins encoded by the rubella virus polyprotein is the E1 envelope glycoprotein. This protein is involved in viral attachment and entry into host cells. The E1 protein is responsible for binding to receptors on the surface of host cells, which allows the virus to enter the cell and begin the process of viral replication.

Another important protein encoded by the rubella virus polyprotein is the RNA-dependent RNA polymerase (RdRp). This protein is responsible for replicating the viral RNA genome during the process of viral replication. The RdRp catalytic domain is responsible for catalyzing the synthesis of new RNA strands using the viral RNA genome as a template. This process is critical for the virus to propagate and cause infection.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.