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  • Title: The HIV-1 protease substitution K55R: a protease-inhibitor-associated substitution involved in restoring viral replication.
    Author: Margerison ES, Maguire M, Pillay D, Cane P, Elston RC.
    Journal: J Antimicrob Chemother; 2008 Apr; 61(4):786-91. PubMed ID: 18252693.
    Abstract:
    OBJECTIVES: The identification and in vitro characterization of novel protease mutations strongly associated with known protease resistance mutations. METHODS: The association between pairs of protease amino acid substitutions was identified using a database of protease sequences derived from protease inhibitor-experienced patients (n = 803). In vitro characterization included drug susceptibility and viral replication studies performed on recombinant viruses harbouring site-directed mutations. RESULTS: The K55R mutation, which is not a natural polymorphism, was identified to be strongly associated with protease mutations M46I/L and to a lesser extent L24I, I54V and V82A/T/S/F. In vitro characterization of the K55R substitution indicated a primary role for this substitution in increasing replicative capacity in the presence of specific protease mutations. CONCLUSIONS: The K55R mutation is a secondary drug resistance mutation that can improve viral replication capacity in the presence of other primary protease mutations.
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