Human and rhesus macaque TRIM5α can bind HIV-1 cores and stabilize CA disassembly

Human immunodeficiency virus type 1 (HIV-1) is a member of the lentiviral subfamily of retroviruses and is characterized by the presence of a conical core (as depicted in Figure 1) and its ability to infect non-dividing cells such as macrophages and resting T-cells of the immune system. The viral core consists of the capsid (CA/p24) protein surrounding an internal viral ribonucleopreotein complex, that contains the viral genome as well as both cellular and viral proteins, including integrase (IN). After fusion of the plasma and viral membranes, the viral core is released into the cytoplasm where the uncoating step occurs. Uncoating, wherein CA disassembles from the viral core, is an essential step in the replication process and perturbations in uncoating can cause defects at various steps in the life cycle, including reverse transcription and nuclear import. Though uncoating is an important, early event, the exact mechanisms governing this step remain poorly understood.