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Structural and biochemical mechanisms of HIV-1 RT drug resistance

  1. Author:
    Boyer, P. L.
    Gao, H. Q.
    Serafianos, S.
    Ding, J.
    Clark, P.
    Clark, A.
    Arnold, E.
    Hughes, S. H.
    1. Year of Conference: 1999
  2. Conference Name: Conference on Retroviruses and Opportunistic Infections
    1. Pages: 218 (abstract no. S33)
  4. Type of Work: Meeting Abstract
  1. Abstract:

    Reverse transcriptase (RT) is the target for a number of clinically important anti-HIV drugs. The approved drugs can be divided into two classes: nucleoside analogs (NRTIs) and nonnucleoside inhibitors (NNRTIs). NRTIs mimic dNTPs but act as chain terminations during viral DNA synthesis. NNRTIs bind to HIV-1 RT near the polymerase active site, altering the structure of the enzyme and inhibiting polymerase activity. Treatment with either NRTIs or NNRTIs selects drug-resistant variants. These variants have changes in RT; in most cases it has been possible to study the mechanisms of resistance using simple biochemical assays. The structure of wild-type HIV-1 RT is reasonably well understood; there are, in addition, structures for several drug-resistant variants. These structures, taken together with the biochemical data, provide useful insights into the mechanisms of resistance, and provide the hope that this information can be used to develop more effective anti-HIV drugs.

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