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Human cellular nucleic acid-binding protein Zn2+ fingers support replication of human immunodeficiency virus type 1 when they are substituted in the nucleocapsid protein

  1. Author:
    McGrath, C. F.
    Buckman, J. S.
    Gagliardi, T. D.
    Bosche, W. J.
    Coren, L. V.
    Gorelick, R. J.

  2. Author Address

    NCI, Aids Vaccine Program, Sci Applicat Int Corp Frederick Inc, Frederick, MD 21702 USA NCI, Aids Vaccine Program, Sci Applicat Int Corp Frederick Inc, Frederick, MD 21702 USA NCI, Dev Therapeut Program, Target Struct Based Drug Discovery Grp, Frederick, MD USA Gorelick RJ NCI, Aids Vaccine Program, Sci Applicat Int Corp Frederick Inc, Frederick, MD 21702 USA
    1. Year: 2003
  2. Journal: Journal of Virology
    1. 77
    2. 15
    3. Pages: 8524-8531
  4. Type of Article: Article
  1. Abstract:

    A family of cellular nucleic acid binding proteins (CNBPs) contains seven Zn2+ fingers that have many of the structural characteristics found in retroviral nucleocapsid (NC) Zn2+ fingers. The sequence of the NH2-terminal NC Zn2+ finger of the pNL4-3 clone of human immunodeficiency virus type 1 (HIV-1) was replaced individually with sequences from each of the seven fingers from human CNBP. Six of the mutants were normal with respect to protein composition and processing, full-length genomic RNA content, and infectivity. One of the mutants, containing the fifth CNBP Zn2+ finger (CNBP-5) packaged reduced levels of genomic RNA and was defective in infectivity. There appear to be defects in reverse transcription in the CNBP-5 infections. Models of Zn2+ fingers were constructed by using computational methods based on available structural data, and atom-atom interactions were determined by the hydropathic orthogonal dynamic analysis of the protein method. Defects in the CNBP-5 mutant could possibly be explained, in part, by restrictions of a set of required atom-atom interactions in the CNBP-5 Zn2+ finger compared to mutant and wild-type Zn2+ fingers in NC that support replication. The present study shows that six of seven of the Zn2+ fingers from the CNBP protein can be used as substitutes for the Zn2+ finger in the NH2-terminal position of HIV-1 NC. This has obvious implications in antiviral therapeutics and DNA vaccines employing NC Zn2+ finger mutants.

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