Vesicular exanthema of swine virus cDNA and Antigen

Vesicular exanthema of swine (VES) is a contagious, infectious disease of swine caused by a virus belonging to the family Picornaviridae. It is characterized by vesicles on the snout, lips and coronary bands of swine. This disease is of worldwide distribution and can cause significant economic losses. Clinical signs usually appear within 5 to 7 days after infection and include fever, lethargy, anorexia, and the formation of vesicles and erosions on the snout, lips, and coronary bands. The virus is spread by direct contact or through contaminated feed or water. Treatment is supportive and includes fluid therapy and antibiotics to control secondary bacterial infections. Vaccines are available to reduce the incidence of disease.

Vesicular exanthema of swine (VESV) is an infectious disease of swine caused by a virus of the same name. The virus is a member of the family Picornaviridae and is closely related to the human enteroviruses. It is highly contagious, and outbreaks can cause significant losses in swine herds. Infection is usually characterized by the formation of vesicles and blisters on the snout and feet of affected animals. The virus is present in the blister fluid, and can be detected using a variety of methods, including antigen-capture ELISA and RT-PCR. Treatment of VESV is limited, and control measures focus on vaccination of susceptible animals, as well as strict biosecurity and quarantine protocols.
Vesicular exanthema of swine virus (VESV) is a contagious viral disease that is found in pigs worldwide. It is caused by a virus from the genus Vesiculovirus, which is part of the family Paramyxoviridae. It is characterized by vesicle formation on the snout, muzzle, and forelimbs of infected pigs. Clinical signs vary depending on the age of the pig, but can include fever, lethargy, anorexia, and swollen lymph nodes. In severe cases, the virus can cause poor growth, lameness, and even death.

The VESV genome is a single-stranded, negative-sense RNA. It encodes eight genes that encode structural and non-structural proteins involved in virus replication and packaging. These proteins are required for the virus to spread between cells and cause disease.

VESV is effectively managed through vaccination and biosecurity measures. Vaccines can be administered to pigs to provide them with immunity to the virus. Biosecurity practices such as quarantining and isolating infected animals, as well as proper sanitation of the environment and equipment, can help to prevent the spread of the virus.

The capsid protein of VESV is a structural protein that forms the outer shell of the virus particle. It plays a critical role in protecting the virus genome and facilitating virus assembly and release. The capsid protein is composed of many copies of a single protein subunit, which assembles into an icosahedral structure.

During the replication cycle of VESV, the capsid protein is synthesized, and the virus RNA genome is packaged inside the capsid. The assembled capsids then move towards the cell membrane and bind to specific receptors on the host cell surface, leading to virus entry.

Once inside the host cell, the virus replicates and produces new viral particles. The capsid protein is involved in the packaging of the newly synthesized viral RNA, and as the virus particles mature, the capsids are assembled around the genome. The mature virus particles are then released from the host cell, allowing the virus to spread to other cells and animals.

Understanding the structure and function of the capsid protein is crucial for developing effective antiviral treatments and vaccines against VESV. Studies of the capsid protein of VESV have also provided insights into the replication mechanisms of other viruses, leading to the development of new antiviral therapies for a range of viral infections.

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.