HIV-1 Rev protein – Rev response element complex (Rev–RRE (sometimes designated as "Rev/RRE"))

The **HIV-1 Rev protein – Rev response element complex** (commonly abbreviated as Rev–RRE) is an essential viral ribonucleoprotein assembly in the life cycle of human immunodeficiency virus type 1 (HIV-1)[1][2][3][4][6]. The **Rev protein** is a regulatory accessory protein (13 kDa) produced early during viral replication. It shuttles into the nucleus, where it specifically binds to the **Rev response element (RRE)**—a highly structured ~350-nucleotide RNA element located within the env region of unspliced and partially spliced viral RNAs[2][3][4]. Multiple Rev molecules oligomerize on the RRE, forming a complex that recruits the host export receptor CRM1/XPO1. This complex mediates the **nuclear export** of intron-containing HIV-1 RNAs, which otherwise would be retained for splicing or degradation[1][3][4][7]. Once exported, these RNAs serve either as templates for viral protein synthesis or as genomic RNA for new virions. The Rev–RRE axis is **indispensable for efficient HIV-1 replication**, and disruption of this pathway halts virus production[2][3][4]. This makes the Rev–RRE interface an attractive, though still experimental, target for antiviral drug development, with approaches including small molecules, peptides, and nucleic acid analogs aimed at blocking the protein–RNA interaction or the nuclear export activity[2][4][6]. Key points: - Both Rev and RRE are unique to retroviruses like HIV-1; they do not have direct human homologs. - Functional Rev–RRE complexes are necessary for late gene expression (Gag, Pol, Env) and for virus assembly and release. - This complex is a primary regulatory checkpoint in the HIV-1 replicative cycle[1][2][3][4][7].

Other names

HIV-1 Rev–RRE complexHIV-1 Rev response element (RRE)HIV-1 Rev proteinRev–RRE ribonucleoprotein complexRev–RRE export complex

Inhibition of Rev binding to the RRE (prevents nuclear export of unspliced/singly spliced viral RNAs); Disruption of Rev oligomerization on RRE (prevents functional complex assembly); Blocking nuclear export pathway by interfering with the Rev–RRE–CRM1 complex formation