Function of HIV Rev

  • Rev is an accessory protein which controls the nuclear export of unspliced and partially spliced viral RNAs from nucleus to cytoplasm [1].

  • Rev multimers bind to the stem-loop structure of Rev response element (RRE) in the env coding region of viral RNA, forming a large oligomeric ribonucleoprotein (RNP) [2].

  • RNP complex interacts with the human export factor CRM1 (exportin 1 or Xpo1) and shuttles through the nuclear pore complex (NPC) from nucleus to cytoplasm.

  • Rev activity exerts a strong influence on HIV-1 RNA transport, translation and packaging [3].

  • Rev is not incorporated in the viral particles [4].

Reference

  1. Fernandes J, Jayaraman B, Frankel A: The HIV-1 Rev response element: an RNA scaffold that directs the cooperative assembly of a homo-oligomeric ribonucleoprotein complex. RNA biology 2012, 9(1):6-11.(Download Article)

  2. Xue B, Mizianty MJ, Kurgan L, Uversky VN: Protein intrinsic disorder as a flexible armor and a weapon of HIV-1. Cellular and molecular life sciences : CMLS 2012, 69(8):1211-1259.(Download Article)

  3. Jeang K-T: Multi-Faceted Post-Transcriptional Functions of HIV-1 Rev. Biology 2012, 1(2):165-174.(Download Article)

  4. Giroud C, Chazal N, Briant L: Cellular kinases incorporated into HIV-1 particles: passive or active passengers? Retrovirology 2011, 8:71.(Download Article)

Sequence

(1) Reference sequence for HIV-1 Rev

  • Strain: HIV-1 subtype B HXB2 (ID: K03455)

  • Fasta format: Download

  • Reference sequence: 

  1       10         20         30         40         50
  |        |          |          |          |          | 
  MAGRSGDSDE ELIRTVRLIK LLYQSNPPPN PEGTRQARRN RRRRWRERQR 
  51      60         70         80         90         100
  |        |          |          |          |          | 
  QIHSISERIL GTYLGRSAEP VPLQLPPLER LTLDCNEDCG TSGTQGVGSP 
  101    110     116
  |        |      | 
  QILVESPTVL ESGTKE

(2) Reference sequence for HIV-2 and SIV Rev

  • Strain: SIV Mac239 (ID: M33262)

  • Fasta format: Download

  • Reference sequence: 

  1       10         20         30         40         50
  |        |          |          |          |          | 
  MSNHEREEEL RKRLRLIHLL HQTNPYPTGP GTANQRRQRK RRWRRRWQQL 
  51      60         70         80         90         100
  |        |          |          |          |          | 
  LALADRIYSF PDPPTDTPLD LAIQQLQNLA IESIPDPPTN TPEALCDPTE 
  101  107
  |     |
  DSRSPQD

(3) Coloring scheme for above amino acids

  1. Amino acids with hydrophobic side chains (normally buried inside the protein core):

    • A - Ala - Alanine

    • I - Ile - Isoleucine

    • L - Leu - Leucine

    • M - Met - Methionine

    • V - Val - Valine

  2. Amino acids with polar uncharged side chains (may participate in hydrogen bonds):

    • N - Asn - Asparagine

    • Q - Gln - Glutamine

    • S - Ser - Serine

    • T - Thr - Threonine

  3. Amino acids with positive charged side chains:

    • H - His - Histidine

    • K - Lys - Lysine

    • R - Arg - Arginine

  4. Amino acids with negative charged side chains:

    • D - Asp - Aspartic acid

    • E - Glu - Glutamic acid

  5. Amino acids with aromatic side chains:

    • F - Phe - Phenylalanine

    • Y - Tyr - Tyrosine

    • W - Trp - Tryptophan

  6. Cysteine: C - Cys - Cysteine

  7. Glycine: G - Gly - Glycine

  8. Proline: P - Pro - Proline

Amino acid variations at HIV-1 Rev

Here, we visualize the prevalence of amino acid variations at the HIV-1 Rev from HIV-1 subtype B.

Protocal of our sequence collection

  • For HIV-1 subtype B, one sequence per patient was extracted from HIV Los Alamos database (www.hiv.lanl.gov/).

  • We removed misclassified sequences or sequences with hypermutations, stop codons, ambiguous nucleotides, which were described in our article [1].

  • We removed sequences conferred partial or full resistance to any of the Rev inhibitors, RT inhibitors and Rev inhibitors using HIVdb V6.0 .

Visualization

Our sequence dataset of HIV-1 subtype B Rev included 4725 sequences. In the following picture, HXB2 indices of individual proteins are shown on top of the colored bars. A consensus amino acid at each position is shown beneath the colored bar. Natural variations are shown below the consensus amino acids; proportions (%) are colored red if they were more than 5%; blue otherwise.


HIV-1 protein interaction patterns.

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Please cite our article:

  1. Guangdi Li, Supinya Piampongsant, Nuno Rodrigues Faria, Arnout Voet, Andrea-Clemencia Pineda-Peña, Ricardo Khouri, Philippe Lemey, Anne-Mieke Vandamme, Kristof Theys. An integrated map of HIV genome-wide variation from a population perspective. Retrovirology 12, 18, doi:10.1186/s12977-015-0148-6 (2015). [PDF] [PubMed Link]

Structure

(1) Secondary structure of HIV-1 Rev

Here, we visualize the secondary structure of HIV-1 Rev using PDBSum (PDB code: 1A30)



(2) Tertiary structure of HIV-1 Rev

Here, we provide a structure movie of Rev using PyMOL V1.7 (PDB code: 1A30). Alpha-helix and beta-strand secondary structures are demonstrated by red .

Localization

(1) Coding region of Rev at the HIV genome


(2) Localization of Rev during the HIV-1 life cycle

Here, we visualize the localization of Rev during the viral life cycle. Red stars indicate the appearance of HIV-1 Rev.


Anti-HIV inhibitor

(1) Drug binding pocket of HIV-1 Rev

Here, we visualize the drug binding pocket of HIV-1 Rev



(2) List of known inhibitors targeting HIV-1 Rev

Here, we summarize the published anti-HIV inhibitors which bind to HIV-1 Rev.



Protein-protein interactions