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A second-site suppressor significantly improves the defective phenotype impolsed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein

  1. Author:
    Tang, S. X.
    Ablan, S.
    Dueck, M.
    Ayala-Lopez, W.
    Soto, B.
    Caplan, M.
    Nagashima, K.
    Hewlett, I. K.
    Freed, E. O.
    Levin, J. G.

  2. Author Address

    NICHHD, Mol Genet Lab, Viral Gene Regulat Sect, NIH, Bethesda, MD 20892 USA. US FDA, Ctr Biol Evaluat & Res, Mol Virol Lab, Bethesda, MD 20892 USA. NCI, Frederick Canc Res & Dev Ctr, HIV Drug Resistance Program, Virus Cell Interact Sect, Frederick, MD 21702 USA. NCI, Frederick Canc Res & Dev Ctr, SAIC Frederick Inc, Image Anal Lab, Frederick, MD 21702 USA.;Levin, JG, NICHHD, Mol Genet Lab, Viral Gene Regulat Sect, NIH, Bldg 6B,Room 216, Bethesda, MD 20892 USA.;levinju@mail.nih.gov
    1. Year: 2007
    2. Date: Mar
  2. Journal: Virology
    1. 359
    2. 1
    3. Pages: 105-115
  4. Type of Article: Article
  5. ISSN: 0042-6822
  1. Abstract:

    The HIV-1 capsid (CA) protein plays an important role in virus assembly and infectivity. Previously, we showed that Ala substitutions in the N-terminal residues Trp23 and Phe40 cause a severely defective phenotype. In searching for mutations at these positions that result in a non-lethal phenotype, we identified one candidate, W23F. Mutant virions contained aberrant cores, but unlike W23A, also displayed some infectivity in a single-round replication assay and delayed replication kinetics in MT-4 cells. Following long-term passage in MT-4 cells, two second-site mutations were isolated. In particular, the W23F/V261 mutation partially restored the wild-type phenotype, including production of particles with conical cores and wild-type replication kinetics in MT-4 cells. A structural model is proposed to explain the suppressor phenotype. These findings describe a novel occurrence, namely suppression of a mutation in a hydrophobic residue that is critical for maintaining the structural integrity of CA and proper core assembly. Published by Elsevier Inc.

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External Sources

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  2. DOI: 10.1016/j.virol.2006.09.027
  3. View record in Web of Science®
  4. WOS: 000244735700012

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