Proteomics/Proteolytic processing/Proteolytic processing of the Human Immunodeficiency Virus type 1
Proteolytic processing of the Human Immunodeficiency Virus type 1
Polyprotein precursors translates the proteins that forms the retroviral particle. One of these precursors has viral protease that processes the precursors itself. This viral protease cleaves the retroviral precursor proteins during the virus assembly. Fully infectious viral particles are produced by precise Protease-mediated precursor processing and if the order of the cleavage changes, it results in the less infectious viral particle. To become active the protease has to be localized along with the requirement of enzyme dimerization. Enzymes come from PR(Protease) domains of GagPol precursors. The processing events are first carried out by the embedded PR, prior to the release from the GagPol precursor.The activated protease domain on one pair of GagPol molecules cleaves initial sites on those same molecules. Further substitutions at the first amino acid in the protease, a proline, lift this constraint and free the protease domain within GagPol to cleave additional native processing sites in the precursor not cleaved by the wild-type embedded protease.