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Mutations in HIV-1 gag and pol Compensate for the Loss of Viral Fitness Caused by a Highly Mutated Protease

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00383709" target="_blank" >RIV/61388963:_____/12:00383709 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1128/AAC.00465-12" target="_blank" >http://dx.doi.org/10.1128/AAC.00465-12</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1128/AAC.00465-12" target="_blank" >10.1128/AAC.00465-12</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Mutations in HIV-1 gag and pol Compensate for the Loss of Viral Fitness Caused by a Highly Mutated Protease

  • Original language description

    During the last few decades, the treatment of HIV-infected patients by highly active antiretroviral therapy, including protease inhibitors (PIs), has become standard. Here, we present results of analysis of a patient-derived, multiresistant HIV-1 CRF02 AG recombinant strain with a highly mutated protease (PR) coding sequence, where up to 19 coding mutations have accumulated in the PR. The results of biochemical analysis in vitro showed that the patient-derived PR is highly resistant to most of the currently used PIs and that it also exhibits very poor catalytic activity. Determination of the crystal structure revealed prominent changes in the flap elbow region and S1/S1' active site subsites. While viral loads in the patient were found to be high, theinsertion of the patient-derived PR into a HIV-1 subtype B backbone resulted in reduction of infectivity by 3 orders of magnitude. Fitness compensation was not achieved by elevated polymerase (Pol) expression, but the introduction of pati

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GAP207%2F11%2F1798" target="_blank" >GAP207/11/1798: HIV protease inhibitors: mechanism of action and resistance development</a><br>

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Antimicrobial Agents and Chemotherapy

  • ISSN

    0066-4804

  • e-ISSN

  • Volume of the periodical

    56

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    11

  • Pages from-to

    4320-4330

  • UT code for WoS article

    000306826300036

  • EID of the result in the Scopus database