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Characterization of HIV-1 integrase N-terminal mutant viruses.

Lloyd AG, Ng YS, Muesing MA, Simon V, Mulder LC

The Aaron Diamond AIDS Research Center 455 First Avenue, New York, NY 10016, USA.

During infection, human immunodeficiency virus type 1 integrase engages a number of molecules and mechanisms, both of viral and cellular origin. In one of such instances, integrase is thought to be degraded by the N-end rule proteasome pathway a process that targets the N-terminal residue of its substrates. Here we describe the properties of HIV-1 viruses in which the first amino acid residue of integrase has been substituted to render it resistant to the N-end rule pathway. As result of this exchange, we observe a set of class I and class II defects that result in a large decrease of viral replication efficiency. Specifically, reverse transcription and integration are the steps that appear to be affected. We propose that the severe deficiency of these mutants exert a strong selective pressure that leads to the near total conservation of the N-terminal residue of integrase in HIV-1, HIV-2 and SIV.

Published 5 March 2007 in Virology, 360(1): 129-35.
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