New insights in the role of nucleoporins: a bridge leading to concerted steps from HIV-1 nuclear entry until integration.
Human Immunodeficiency virus type 1 (HIV-1), as well as many other viruses that depend on nuclear entry for replication, has developed an evolutionary strategy to dock and translocate through the nuclear pore complex (NPC). In particular, the nuclear pore is not a static window but it is a dynamic structure involved in many vital cellular functions, as nuclear import/export, gene regulation, chromatin organization and genome stability. This review aims to shed light on viral mechanisms developed by HIV-1 to usurp cellular machinery to favor viral gene expression and their replication. In particular, it will be reviewed both what is known and what is speculated about the link between HIV translocation through the nuclear pore and the proviral integration in the host chromatin.
Molecular Virology and Vaccinology Unit, CNRS UMR 3569, Department of Virology, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France. Electronic address: francesca.di-nunzio@pasteur.fr.
Francesca
F
Di Nunzio
D015497:HIV-1 / Q000502:physiology*; D006801:Humans; D028861:Nuclear Pore Complex Proteins / Q000378:metabolism*; D016662:Virus Integration
D028861:Nuclear Pore Complex Proteins
Capsid (CA); Cyclophilin A (CypA); Cyclosporin A (CsA); Nuclear pore complex (NPC); Nucleoporins (Nups); Pre-integration complex (PIC)