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Replication-dependent fitness recovery of Human Immunodeficiency virus 1 harbouring mutations of Asn17 of the nucleocapsid protein

  1. Author:
    Tozser, J.
    Shulenin, S.
    Young, M. R.
    Briggs, C. J.
    Oroszlan, S.

  2. Author Address

    NCI, Frederick, MD 21701 USA. Debrecen Univ Med, Res Ctr Mol Med, Dept Biochem & Mol Biol, H-4012 Debrecen, Hungary.;Oroszlan, S, NCI, Frederick, MD 21701 USA.;oroszlans@mail.ncifcrf.gov
    1. Year: 2006
    2. Date: Apr
  2. Journal: Journal of General Virology
    1. 87
    2. Pages: 961-965
  4. Type of Article: Article
  5. ISSN: 0022-1317
  1. Abstract:

    The genetic stability of attenuated Human immunodeficiency virus 1 (HIV-1) variants harbouring mutations (Gly or Lys) of Asn17, the protease-cleavage site of the proximal zinc finger of the nucleocapsid protein, was studied. All possible codons for the Gly mutants were tested as starting sequences. Long-term replication assays revealed that the mutants were unstable; mutations of Glyl 7 to Arg, Ala, Ser and Cys, as well as a Lys17Asn reversion, were observed. Replication kinetic assays in H9 cells revealed that the replication of Ala, Ser and Arg mutants was improved substantially compared with the Gly variant; the infectivity of Ala17 and Ser17 viruses was equal to, and that of Arg 17 was almost equal to, the infectivity of the wild-type virus. Kinetic analysis of the cleavage of oligopeptides representing the corresponding nucleocapsid-cleavage sites revealed that all mutations improved cleavability, in good agreement with the previously proposed role of nudeocapsid cleavage in HIV-1 replication.

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External Sources

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  2. DOI: 10.1099/vir.0.81473-0
  3. View record in Web of Science®
  4. WOS: 000236446400026

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