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- W2034897068 abstract "Development of novel therapeutic targets against HIV-1 is a high research priority owing to the serious clinical consequences associated with acquisition of resistance to current antiretroviral drugs. The HIV-1 structural protein Gag represents a potential new therapeutic target as it plays a central role in virus particle production yet is not targeted by any of the antiretroviral drugs approved at present. The Gag polyprotein precursor multimerizes to form immature particles that bud from the infected cell. Concomitant with virus release, the Gag precursor undergoes proteolytic processing by the viral protease to generate the mature Gag proteins, which include capsid (CA). Once liberated from the Gag polyprotein precursor, CA molecules interact to reassemble into a condensed conical core, which organizes the viral RNA genome and several viral proteins to facilitate virus replication in the next round of infection. Correct Gag proteolytic processing and core assembly are therefore essential for virus infectivity. In this review, we discuss new strategies to inhibit maturation by targeting proteolytic cleavage sites in Gag or CA–CA interactions required for core formation. The identification and development of lead maturation inhibitors are highlighted." @default.
- W2034897068 created "2016-06-24" @default.
- W2034897068 creator A5054660762 @default.
- W2034897068 creator A5076272684 @default.
- W2034897068 creator A5076741157 @default.
- W2034897068 date "2009-06-17" @default.
- W2034897068 modified "2023-10-18" @default.
- W2034897068 title "Virus maturation as a new HIV-1 therapeutic target" @default.
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