Saimiriine herpesvirus cDNA and Antigen

Saimiriine herpesvirus is a herpesvirus that infects squirrel monkeys. It is a member of the subfamily Alphaherpesvirinae and is closely related to other primates. Symptoms of infection include respiratory, dermatological, and neurological disorders. Treatment options are limited, but antiviral medications can help reduce the severity of the disease.

Saimiriine herpesvirus (Saimiriine herpesvirus 1, SHV-1) is an alphaherpesvirus that infects certain species of squirrel monkeys (Saimiri spp.). SHV-1 is the only species of the genus Saimiriine herpesvirus. SHV-1 causes a variety of clinical signs including conjunctivitis, rhinitis, respiratory disease, encephalitis, and death in infected animals. Antigenic components of SHV-1, including the major capsid protein, glycoprotein B, and thymidine kinase, are used in serological tests to detect antibodies to the virus in infected animals. These components are also used in vaccine development and in the development of diagnostic assays.

Saimiriine herpesvirus (SaHV) is a virus that infects New World monkeys (tribe Saimiri). The SaHV genome is a linear, double-stranded DNA molecule approximately 130 kb in size. The SaHV genome encodes more than 100 proteins involved in various cellular processes, including transcription, replication, and assembly. Several genes have been identified as involved in the virus’s pathogenesis, including a major capsid protein, an envelope glycoprotein, and a major envelope protein. In addition, several other proteins have been identified as putative virulence factors. The SaHV genome also encodes several non-structural proteins, including a helicase and an RNA-dependent RNA polymerase, which are involved in viral gene expression and replication.

Envelope glycoprotein B (gB) is a key protein of Saimiriine herpesvirus 1 and 2 that plays an important role in viral entry into host cells. This protein is responsible for binding to cellular receptors and facilitating the fusion of the viral envelope with the host cell membrane.

Immediate early 14-C protein (IE14-C) is another important protein of Saimiriine herpesvirus 1 and 2. It is involved in the regulation of viral gene expression and plays a crucial role in the establishment of viral latency in host cells.

Surface glycoprotein CD59 homolog (CD59) is a viral protein that shares structural similarity with the host protein CD59. CD59 plays a critical role in evading the host immune response by inhibiting the complement system, a key component of the innate immune response.

Major capsid protein (MCP) and Capsid protein VP26 are two proteins that are involved in the formation of the viral capsid, which protects the viral genome during transmission. MCP is a major structural protein of the viral capsid, while VP26 is involved in stabilizing the capsid structure.

Immediate-early protein IE-G is a viral protein that is involved in the regulation of viral gene expression. It is produced immediately after viral infection and plays a crucial role in initiating the viral replication cycle.

Immediate early gene 13 protein (IE13) is another important protein of Saimiriine herpesvirus 1 and 2. It is involved in the regulation of viral gene expression and plays a critical role in viral latency and reactivation.

In summary, Saimiriine herpesvirus 1 and 2 have several key proteins, including Envelope glycoprotein B, Immediate early 14-C protein, Surface glycoprotein CD59 homolog, Major capsid protein, Immediate-early protein IE-G, Capsid protein VP26, and Immediate early gene 13 protein, that play crucial roles in viral replication and pathogenesis.

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.