Western equine encephalitis virus cDNA and Antigen

Western equine encephalitis virus (WEEV) is a mosquito-borne virus that is part of the Alphavirus genus of the Togaviridae family. WEEV is endemic to the western hemisphere and is found primarily in North and South America. It is most active in the summer and fall months. Symptoms of WEEV infection can range from mild to severe. Mild cases may cause a fever and headache, while severe cases may cause encephalitis (swelling of the brain) and even death. Treatment for WEEV infection is supportive care and there is no specific antiviral therapy. The best way to prevent WEEV infection is to avoid mosquito bites.

Western equine encephalitis virus (WEEV) is a mosquito-borne virus that can cause severe neurological disease in humans and horses. The infection is most diagnosed through a blood test that looks for antibodies to the virus. The most reliable test is an enzyme-linked immunosorbent assay (ELISA) that looks for WEEV antigen. WEEV antigen is a protein found on the surface of the virus and is used by the body’s immune system to detect the presence of the virus.

Western equine encephalitis virus (WEEV) is a single-stranded, negative-sense, enveloped RNA virus that belongs to the genus Alphavirus in the family Togaviridae. The WEEV genome is approximately 11.7-11.8 kb in length and contains five structural genes flanked by two non-translated regions at the 5′ and 3′ ends. The structural genes encode the following proteins: the viral capsid (C), envelope (E3), envelope (E2), envelope (E1), and nonstructural (nsP3), respectively. The non-structured regions contain several conserved motifs and sequences involved in replication and transcription.

The envelope glycoprotein E1 is a major surface protein of the virus and plays a critical role in mediating virus entry into host cells. The nsP2 and nsP3 proteins are non-structural proteins involved in viral RNA replication and modulation of host cell function, respectively. The C-protein is a structural protein that plays a role in virion assembly and maturation. The E2-protein is a surface glycoprotein that interacts with host cells and is a target of the host immune response. The E1-protein is another surface glycoprotein that is involved in virus entry and fusion with host cells.

Understanding the structure and function of these key proteins is important for developing effective therapies and vaccines against WEEV. Research into these proteins is ongoing, and new insights into their roles in WEEV pathogenicity and immune evasion may lead to new strategies for preventing and treating this dangerous disease.

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.