Lactate dehydrogenase elevating virus cDNA and Antigen

Lactate Dehydrogenase Elevating Virus (LDV) is a type of virus that can infect various species of rodents, including mice and rats. LDV is known for its ability to cause an elevation in the levels of lactate dehydrogenase (LDH) in infected animals, leading to a condition called LDH elevating disease. The virus is spread through contact with infected tissues or fluids and can cause a range of symptoms, including weight loss, lethargy, and death. LDV is not known to cause disease in humans. However, it is important to understand the biology of LDV and its impact on infected animals for several reasons, including controlling outbreaks in laboratory animal populations and improving animal welfare.

Lactate dehydrogenase elevating virus (LDV) is a virus that can cause both acute and chronic diseases in mice. The LDV antigen is a protein that is present on the surface of the virus, and it can be used as a marker to identify LDV infection. In infected mice, antibodies against the LDV antigen can be detected, and this is a common method used to diagnose LDV infection in colonies of mice.

The lactate dehydrogenase elevating virus (LDV) genome is the genetic material of the virus, which is made up of RNA. The LDV genome is a linear, single-stranded RNA molecule that encodes several viral proteins, including the structural proteins required for virus assembly and the enzymes involved in virus replication. The precise size and sequence of the LDV genome can vary between different strains of the virus. Understanding the LDV genome is important for understanding the biology of the virus and for developing strategies for preventing and controlling LDV infections.

Lactate dehydrogenase elevating virus (LDV) is a single-stranded RNA virus that primarily infects rodents, causing persistent infections and immunosuppression. The virus contains several proteins that play important roles in its replication and pathogenesis.

One of these proteins is non-structural protein 12 (nsp12), which is an RNA-dependent RNA polymerase and is essential for viral RNA synthesis. Another non-structural protein, nsp11, is involved in viral RNA replication and plays a role in suppressing the host immune response.

The capsid protein of LDV forms the outer shell of the virus and protects the viral genome. The minor structural glycoprotein and primary envelope glycoprotein are both involved in the process of viral entry into host cells and the induction of the host immune response.

Protein X is a unique protein found in LDV and related viruses, and its function is not well understood. Studies have shown that Protein X can modulate the host immune response and may also play a role in virus assembly and replication.

Understanding the functions and interactions of these LDV proteins is important for the development of effective treatments and vaccines for LDV-induced diseases. In addition, studying LDV may provide insights into the pathogenesis of other viruses that are closely related to LDV, including the human coronavirus that causes severe acute respiratory syndrome (SARS).

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.