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Amino acid deletion at codon 67 and Thr-to-Gly change at codon 69 of human immunodeficiency virus type 1 reverse transcriptase confer novel drug resistance profiles

  1. Author:
    Imamichi, T.
    Murphy, M. A.
    Imamichi, H.
    Lane, H. C.

  2. Author Address

    NCI, Lab Mol Retrovirol, Clin Serv Program, SAIC Frederick, Bldg 550, Room 126, POB B, Frederick, MD 21702 USA. NCI, Lab Mol Retrovirol, Clin Serv Program, SAIC Frederick, Frederick, MD 21702 USA. NIAID, Immunoregulat Lab, Bethesda, MD 20892 USA. Imamichi T NCI, Lab Mol Retrovirol, Clin Serv Program, SAIC Frederick, Bldg 550, Room 126, POB B, Frederick, MD 21702 USA.
    1. Year: 2001
  2. Journal: Journal of Virology
    1. 75
    2. 8
    3. Pages: 3988-3992
  4. Type of Article: Article
  1. Abstract:

    The potential rules of an amino acid deletion at codon 67 (Delta 67) and a Thr-to-Gly change at codon 69 (T69G) in the reverse transcriptase of human immunodeficiency virus (HIV) type 1 in drug sensitivity and relative replication fitness were studied. Our results suggest that the Delta 67 and T69G changes can be categorized as mutations associated with multidrug resistance. The combination of both mutations with an L74I change (Delta 67+T69G/L74I) leads to a novel 3'-azido-3'- deoxythymidine resistance motif and compensates for impaired HIV replication.

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