Herpes Simplex Virus-2 (HSV-2) is a member of the Herpesviridae family, primarily known for causing genital herpes. The virus has a complex structure, consisting of an envelope, tegument, capsid, and core. Among the various proteins encoded by HSV-2, the tegument proteins play a crucial role in the virus’s life cycle. One such tegument protein is VP13/14, encoded by the UL47 gene.
VP13/14 is a major structural component of the virion tegument, the compartment located between the capsid and the virus envelope . The protein has apparent masses of 82 and 81 kDa, respectively, and is posttranslationally modified by phosphorylation, nucleotidylylation, and glycosylation . These modifications are believed to contribute to the protein’s functional diversity.
VP13/14 is capable of nuclear shuttling, a property that is attributed to its nuclear localization signals (NLS) and nuclear export signals (NES) . The NLS of VP13/14 contains two runs of four arginine residues, similar to the arginine-rich NLS of retrovirus transactivator proteins like Tat, Rev, and Rex . Additionally, VP13/14 has three leucine-rich stretches in its C-terminal half, which resemble the NES of Rev and Rex . This nuclear shuttling capability is significant during virus entry and later stages of infection when large amounts of newly synthesized VP13/14 are present within the cell .
VP13/14 is also a major target antigen for T cells obtained from vitreous fluid samples of patients with HSV-induced acute retinal necrosis (ARN) . The protein contains specific epitopes recognized by CD4+ T cells, indicating its role in the local inflammatory response during HSV infection . This immunological significance makes VP13/14 a potential target for therapeutic interventions.
Recombinant VP13/14 proteins are produced using various expression systems to study their structure, function, and immunogenicity. These recombinant proteins are valuable tools for understanding the molecular mechanisms of HSV-2 infection and developing potential vaccines and antiviral therapies.