HAV VP4-VP2 Protein was purified by proprietary chromatographic technique.
Hepatitis A Virus (HAV) is a member of the Picornaviridae family, known for causing acute hepatitis in humans. The virus has a positive-sense RNA genome encapsidated in a shell formed by 60 copies of at least three viral proteins: VP1, VP2, and VP3 . A small structural protein, VP4, plays a crucial role in the assembly and stability of the viral capsid .
The HAV capsid is composed of four structural proteins: VP1, VP2, VP3, and VP4 . These proteins are essential for the formation and stability of the viral particle. The mature icosahedral capsid is composed of 12 pentamers, each consisting of five copies of these four proteins . The smallest of these proteins, VP4, is located on the inside of the capsid shell, facing the viral RNA genome .
The assembly of the HAV capsid is a complex process that involves the proteolytic processing of a precursor polyprotein. VP4 and VP2 play distinct roles in this process . VP4 is liberated during the final step of capsid maturation and is found on the inside of the capsid shell . The myristoylated N-terminus of VP4 is located below the 5-fold vertices, while its C-terminus is found at the 3-fold axis . VP2, on the other hand, interacts with VP3 and neighboring protomers at the 2-fold axis .
Recombinant VP4-VP2 refers to the use of recombinant DNA technology to produce these proteins in a laboratory setting. This approach allows researchers to study the individual roles of these proteins in capsid assembly and stability. By expressing VP4 and VP2 recombinantly, scientists can investigate their interactions and the signals required for the assembly of viral particles .
Understanding the roles of VP4 and VP2 in HAV capsid assembly has several important applications: