Usutu virus cDNA and Antigen

Usutu virus (USUV) is a mosquito-borne flavivirus that was first identified in South Africa in 1959. It is widely distributed in Africa and has also been reported in Europe. USUV is known to cause disease in birds, including large-scale die-offs in wild birds, and it has also been associated with human encephalitis (inflammation of the brain). The symptoms of USUV infection can range from mild flu-like symptoms to severe neurological disease. In birds, USUV infection can cause significant mortality, particularly in certain species such as the common blackbird. Control of USUV in birds and humans relies on reducing mosquito populations and limiting exposure to infected mosquitoes using insect repellents and personal protective measures. There is currently no specific treatment for USUV infection in humans or birds.

The antigen of Usutu virus (USUV) refers to a protein or other molecule present on the surface of the virus that triggers an immune response from the host (human or bird). The presence of USUV antigens can be used to diagnose infection with the virus and to monitor the effectiveness of a vaccine. In a vaccine, the antigen is typically a weakened or inactivated form of the virus, or a piece of the virus (such as a protein), which can stimulate the immune system to produce antibodies that protect against future infection. The development of USUV antigens has been important for improving the diagnosis and control of USUV infections in humans and birds.

The genome of Usutu virus (USUV) is a single-stranded RNA molecule that encodes the genetic information necessary for the replication and survival of the virus. USUV is a member of the flavivirus genus, which includes other well-known viruses such as dengue fever, yellow fever, and West Nile virus. The USUV genome is approximately 11 kilobases in length and contains a single open reading frame that encodes the viral proteins necessary for replication. The study of the USUV genome has provided important insights into the evolution and diversity of this virus and has helped to develop strategies for controlling its spread and impact on bird and human health. Understanding the USUV genome has also been crucial for the development of effective vaccines and antiviral therapies.

USUV encodes several structural and non-structural proteins, of which the core protein C, protein M, envelope protein, NS1, NS2a, and NS4a are critical components.

The core protein C is a structural protein that forms the viral nucleocapsid. The C protein is responsible for binding to the viral RNA and interacting with the other structural proteins to form the mature virus particle.

The protein M, also known as the membrane protein, is another structural protein that is found in the viral envelope. The M protein interacts with the envelope protein and helps to anchor the viral envelope to the nucleocapsid.

The envelope protein, also known as the E protein, is a critical component of USUV’s replication cycle. The E protein plays a key role in virus entry into host cells by binding to receptors on the host cell surface and mediating virus fusion with the host cell membrane. The E protein is also involved in virus assembly and budding.

The non-structural proteins of USUV include NS1, NS2a, and NS4a. NS1 is a multifunctional protein that is involved in virus replication, assembly, and immune evasion. NS2a plays a role in virus replication by interacting with other viral proteins and host factors. NS4a is involved in virus assembly and release, but its precise role in USUV replication is not fully understood.

Understanding the structure and function of USUV’s critical proteins is important for developing effective vaccines and antiviral therapies against this emerging pathogen. Moreover, studying USUV’s proteins and their interactions with host factors may provide insights into the pathogenesis of other flaviviruses that affect both animals and humans.

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.