Skip NavigationSkip to Content
Return Return to Search Results

Polymorphisms in Gag spacer peptide 1 confer varying levels of resistance to the HIV-1 maturation inhibitor bevirimat

  1. Author:
    Adamson, C. S.
    Sakalian, M.
    Salzwedel, K.
    Freed, E. O.

  2. Author Address

    [Adamson, Catherine S.; Freed, Eric O.] NCI, Virus Cell Interact Sect, HIV Drug Resistance Program, Frederick, MD 21702 USA. [Sakalian, Michael; Salzwedel, Karl] Panacos Pharmaceut Inc, Gaithersburg, MD 20877 USA. [Adamson, Catherine S.] Univ St Andrews, Bute Med Sch, St Andrews KY16 9TS, Fife, Scotland.;Adamson, CS, NCI, Virus Cell Interact Sect, HIV Drug Resistance Program, Frederick, MD 21702 USA.;catherine.adamson@st-andrews.ac.uk
    1. Year: 2010
    2. Date: Apr
  2. Journal: Retrovirology
    1. 7
    2. Pages: 8
  4. Type of Article: Article
  5. Article Number: 36
  6. ISSN: 1742-4690
  1. Abstract:

    Background: The maturation inhibitor bevirimat (BVM) potently inhibits human immunodeficiency virus type 1 (HIV-1) replication by blocking capsid-spacer peptide 1 (CA-SP1) cleavage. Recent clinical trials demonstrated that a significant proportion of HIV-1-infected patients do not respond to BVM. A patient's failure to respond correlated with baseline polymorphisms at SP1 residues 6-8. Results: In this study, we demonstrate that varying levels of BVM resistance are associated with point mutations at these residues. BVM susceptibility was maintained by SP1-Q6A, -Q6H and -T8A mutations. However, an SP1-V7A mutation conferred high-level BVM resistance, and SP1-V7M and T8 Delta mutations conferred intermediate levels of BVM resistance. Conclusions: Future exploitation of the CA-SP1 cleavage site as an antiretroviral drug target will need to overcome the baseline variability in the SP1 region of Gag.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1186/1742-4690-7-36
  3. View record in Web of Science®
  4. WOS: 000278330800001

Library Notes

  1. Fiscal Year: FY2009-2010
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel