The Choreography of HIV-1 Proteolytic Processing and Virion Assembly

摘要: Abstract HIV-1 has been the target of intensive research at molecular and biochemical levels for >25 years. Collectively, this work led to a detailed understanding viral replication development 24 approved drugs that have five different targets on various proteins one cellular (CCR5). Although most enzymatic activities, our knowledge so much life cycle is leading us into other types inhibitors can block or disrupt protein-protein interactions. Viruses compact genomes employ strategy using small number form repeating structures enclose space (i.e. condensing genome inside protein shell), thus minimizing need large coding capacity. This creates relatively critical interactions are essential replication. For HIV-1, Gag role polyprotein precursor contains all structural virion: matrix, capsid, spacer peptide 1, nucleocapsid, 2, p6 (which protein-binding domains interact with host during budding). Similarly, Gag-Pro-Pol encodes but now includes enzymes: protease, reverse transcriptase (with its associated RNase H activity), integrase. substrates which responsible cleaving these precursors their mature fully active forms (see Fig. 1A).