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

The Journal of General Virology
József TözsérStephen Oroszlan

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 Gly17 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 Arg17 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 nucleocapsid cleavage in HIV-1 replication.

References

Aug 30, 1991·Biochemical and Biophysical Research Communications·C BaboonianJ Merson
Aug 1, 1991·Protein Engineering·M M RobertsS Oroszlan
Apr 28, 1989·Biochemical and Biophysical Research Communications·M M Roberts, S Oroszlan
Jul 25, 1995·Nucleic Acids Research·M A MartínezS Wain-Hobson
Feb 15, 2001·Journal of Medical Virology·T GotoK Sano
Jul 23, 2003·Current Pharmaceutical Design·J Tözsér, S Oroszlan
Jun 9, 2004·The International Journal of Biochemistry & Cell Biology·Carole BampiJean-Luc Darlix
Dec 8, 2004·Current Topics in Medicinal Chemistry·Rabi Ann Musah

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