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HIV-1 Capsid-Targeting Domain of Cleavage and Polyadenylation Specificity Factor 6

  1. Author:
    Lee, K.
    Mulky, A.
    Yuen, W.
    Martin, T. D.
    Meyerson, N. R.
    Choi, L.
    Yu, H.
    Sawyer, S. L.
    KewalRamani, V. N.

  2. Author Address

    [Lee, KyeongEun; Mulky, Alok; Yuen, Wendy; Martin, Thomas D.; Choi, Laura; Yu, Hyun; KewalRamani, Vineet N.] NCI, HIV Drug Resistance Program, Frederick, MD 21701 USA. [Yuen, Wendy] SAIC Frederick, Basic Sci Program, Frederick, MD USA. [Meyerson, Nicholas R.; Sawyer, Sara L.] Univ Texas Austin, Sect Mol Genet & Microbiol, Inst Cellular & Mol Biol, Austin, TX 78712 USA.;KewalRamani, VN (reprint author), NCI, HIV Drug Resistance Program, Frederick, MD 21701 USA;vineet@mail.nih.gov
    1. Year: 2012
    2. Date: Apr
  2. Journal: Journal of Virology
    1. 86
    2. 7
    3. Pages: 3851-3860
  4. Type of Article: Article
  5. ISSN: 0022-538X
  1. Abstract:

    The antiviral factor CPSF6-358 restricts human immunodeficiency virus type 1 (HIV-1) infection through an interaction with capsid (CA), preventing virus nuclear entry and integration. HIV-1 acquires resistance to CPSF6-358 through an N74D mutation of CA that impairs binding of the antiviral factor. Here we examined the determinants within CPSF6-358 that are necessary for CA-specific interaction. Residues 314 to 322 include amino acids that are essential for CPSF6-358 restriction of HIV-1. Fusion of CPSF6 residues 301 to 358 to rhesus TRIM5 alpha is also sufficient to restrict wild-type but not N74D HIV-1. Restriction is lost if CPSF6 residues in the amino acid 314 to 322 interaction motif are mutated. Examination of the CA targeting motif in CPSF6-358 did not reveal evidence of positive selection. Given the sensitivity of different primate lentiviruses to CPSF6-358 and apparent conservation of this interaction, our data suggest that CPSF6-358-mediated targeting of HIV-1 could provide a broadly effective antiviral strategy.

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External Sources

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  2. DOI: 10.1128/jvi.06607-11
  3. View record in Web of Science®
  4. WOS: 000301371500042

Library Notes

  1. Fiscal Year: FY2011-2012
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