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The interdomain linker region of HIV-1 capsid protein is a critical determinant of proper core assembly and stability

  1. Author:
    Jiang, J. Y.
    Ablan, S. D.
    Derebail, S.
    Hercik, K.
    Soheilian, F.
    Thomas, J. A.
    Tang, S. X.
    Hewlett, I.
    Nagashima, K.
    Gorelick, R. J.
    Freed, E. O.
    Levin, J. G.

  2. Author Address

    [Jiang, JY; Derebail, S; Hercik, K; Levin, JG] Eunice Kennedy Shriver Natl Inst Child Hlth, Sect Viral Gene Regulat, Program Genom Differentiat, NIH, Bethesda, MD 20892 USA. [Ablan, SD; Freed, EO] NCI, Virus Cell Interact Sect, HIV Drug Resistance Program, Frederick, MD 21702 USA. [Soheilian, F; Nagashima, K] NCI, Image Anal Lab, SAIC Frederick Inc, Frederick, MD 21702 USA. [Thomas, JA; Gorelick, RJ] NCI, AIDS & Canc Virus Program, SAIC Frederick Inc, Frederick, MD 21702 USA. [Tang, SX; Hewlett, I] US FDA, Mol Virol Lab, Ctr Biol Evaluat & Res, Bethesda, MD 20892 USA.;Levin, JG (reprint author), Eunice Kennedy Shriver Natl Inst Child Hlth, Sect Viral Gene Regulat, Program Genom Differentiat, NIH, Bldg 6B,Room 216,6 Ctr Dr, Bethesda, MD 20892 USA;levinju@mail.nih.gov
    1. Year: 2011
    2. Date: Dec
  2. Journal: Virology
    1. 421
    2. 2
    3. Pages: 253-265
  4. Type of Article: Article
  5. ISSN: 0042-6822
  1. Abstract:

    The HIV-1 capsid protein consists of two independently folded domains connected by a flexible peptide linker (residues 146-150), the function of which remains to be defined. To investigate the role of this region in virus replication, we made alanine or leucine substitutions in each linker residue and two flanking residues. Three classes of mutants were identified: (i) S146A and T148A behave like wild type (WT); (ii) Y145A, 1150A, and L151A are noninfectious, assemble unstable cores with aberrant morphology, and synthesize almost no viral DNA; and (iii) P147L and S149A display a poorly infectious, attenuated phenotype. Infectivity of P147L and S149A is rescued specifically by pseudotyping with vesicular stomatitis virus envelope glycoprotein. Moreover, despite having unstable cores, these mutants assemble WT-like structures and synthesize viral DNA, although less efficiently than WT. Collectively, these findings demonstrate that the linker region is essential for proper assembly and stability of cores and efficient replication. Published by Elsevier Inc.

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External Sources

  1. View Full Text
  2. DOI: 10.1016/j.virol.2011.09.012
  3. View record in Web of Science®
  4. WOS: 000297183900019

Library Notes

  1. Fiscal Year: FY2011-2012
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