Norwalk virus cDNA and Antigen

Norwalk virus, also known as Norovirus, is a virus that causes acute gastroenteritis in humans. Symptoms of Norwalk virus include vomiting, diarrhea, abdominal cramps, and occasionally fever. It is highly contagious and can be spread through contact with an infected person, contaminated food, or water.

Norwalk virus is a type of virus that causes a common type of gastroenteritis known as Norovirus. The Norwalk virus antigen is a protein that is found on the surface of the virus. This antigen is used in diagnostic tests to detect the virus in a sample. The antigen is also used to create vaccines to protect against infection.

Norwalk virus is a member of the family Caliciviridae, and the genome of Norwalk virus consists of a single-stranded, positive-sense RNA molecule that is approximately 7.5 kb in size. This genome encodes three open reading frames (ORFs). The first ORF encodes a polyprotein that is proteolytically cleaved into four capsid proteins (VP1, VP2, VP3, and VP4) as well as two nonstructural proteins (NS1 and NS2). The second ORF encodes a glycoprotein precursor that is cleaved into two mature glycoproteins (G1 and G2). The third ORF is expressed from a subgenomic mRNA and encodes a small basic protein (VPg).

The Capsid protein VP1 is a structural protein that forms the outer shell of the Norwalk virus. It plays a critical role in the attachment of the virus to host cells and in the initiation of the infection process.

Protein p48 is a nonstructural protein that is involved in the replication of the Norwalk virus genome. It interacts with other viral proteins to facilitate the synthesis of viral RNA and the production of new virus particles.

Protein p22 is another nonstructural protein that is involved in the replication of the Norwalk virus genome. It interacts with other viral and host proteins to facilitate the translation of viral RNA into viral proteins.

The Viral genome-linked protein is a nonstructural protein that is covalently linked to the Norwalk virus genome. It is involved in the translation of viral RNA into viral proteins and plays a role in the assembly of new virus particles.

The 3C-like protease is a nonstructural protein that is involved in the processing of viral polyproteins into functional viral proteins. It cleaves the polyproteins at specific sites to release individual viral proteins.

The Minor structural protein is a protein that is present in low quantities in the Norwalk virus particle. Its function is not well understood, but it is believed to play a role in the assembly and release of new virus particles.

NLV Capsid protein is a structural protein found in Norwalk-like viruses. It is involved in the formation of the virus’s outer shell and plays a critical role in the virus’s attachment to host cells.

Understanding the functions and interactions of these various Norwalk virus proteins is critical for developing effective treatments and vaccines against the virus. Research in this area is ongoing, with the hope of finding new ways to prevent and treat this highly contagious and persistent virus.

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.