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AntibodySystem
Recombinant Proteins
Recombinant proteins are proteins that are artificially produced through genetic engineering techniques. These proteins have a wide range of applications in various fields, including medicine, biotechnology, and agriculture. One such recombinant protein is the Recombinant ASFV I177L Protein, which has gained significant attention in recent years due to its potential as an antigen for the development of vaccines against African Swine Fever Virus (ASFV).
The Recombinant ASFV I177L Protein is a 177 amino acid protein that is derived from the I177L gene of the African Swine Fever Virus. This protein is composed of a single polypeptide chain with a molecular weight of approximately 20 kDa. The protein has a well-defined three-dimensional structure, which has been elucidated through X-ray crystallography. It consists of two domains, a large domain, and a small domain, connected by a flexible linker region. The large domain is responsible for the protein’s enzymatic activity, while the small domain is involved in protein-protein interactions.
The Recombinant ASFV I177L Protein is a highly active protein with multiple enzymatic functions. It belongs to the superfamily of metal-dependent hydrolases and exhibits phospholipase A2 (PLA2) and lysophospholipase (LPL) activities. These activities are essential for the virus’s replication and pathogenesis as they play a crucial role in the virus’s entry into the host cell and the release of viral particles from infected cells.
The PLA2 activity of the Recombinant ASFV I177L Protein is responsible for the hydrolysis of phospholipids, which are critical components of cell membranes. This activity allows the virus to enter the host cell by disrupting the cell membrane, facilitating the fusion of the virus with the cell membrane. The LPL activity of the protein is involved in the release of viral particles from infected cells, which is essential for the spread of the virus in the host.
The Recombinant ASFV I177L Protein has gained significant attention as a potential antigen for the development of vaccines against ASFV. The protein’s crucial role in the virus’s replication and pathogenesis makes it an ideal target for vaccine development. By targeting this protein, the vaccine can effectively prevent the virus’s entry into host cells and its spread within the host.
Several studies have demonstrated the effectiveness of the Recombinant ASFV I177L Protein as an antigen for vaccine development. In one study, the protein was used to develop a subunit vaccine, which showed promising results in protecting pigs against ASFV infection. Another study used the protein to develop a DNA vaccine, which induced a strong immune response in pigs and provided protection against the virus.
Apart from its application in vaccine development, the Recombinant ASFV I177L Protein also has potential in diagnostic tests for ASFV. The protein’s enzymatic activities make it an ideal candidate for the development of sensitive and specific diagnostic assays for the virus.
In conclusion, the Recombinant ASFV I177L Protein is a highly active protein with multiple enzymatic functions. Its well-defined structure and crucial role in the virus’s replication and pathogenesis make it an ideal target for vaccine development against ASFV. With further research and development, this protein has the potential to play a significant role in controlling and preventing the spread of ASFV, which is a significant threat to the global swine industry.
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