Non-Cleavage Site Gag Mutations in Amprenavir-Resistant Human Immunodeficiency Virus Type 1 (HIV-1) Predispose HIV-1 to Rapid Acquisition of Amprenavir Resistance but Delay Development of Resistance to Other Protease Inhibitors
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چکیده
منابع مشابه
Resistance mechanism of human immunodeficiency virus type-1 protease to inhibitors: A molecular dynamic approach
Human immunodeficiency virus type 1 (HIV-1) protease inhibitors comprise an important class of drugs used in HIV treatments. However, mutations of protease genes accelerated by low fidelity of reverse transcriptase yield drug resistant mutants of reduced affinities for the inhibitors. This problem is considered to be a serious barrier against HIV treatment for the foreseeable future. In this st...
متن کاملresistance mechanism of human immunodeficiency virus type-1 protease to inhibitors: a molecular dynamic approach
human immunodeficiency virus type 1 (hiv-1) protease inhibitors comprise an important class of drugs used in hiv treatments. however, mutations of protease genes accelerated by low fidelity of reverse transcriptase yield drug resistant mutants of reduced affinities for the inhibitors. this problem is considered to be a serious barrier against hiv treatment for the foreseeable future. in this st...
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The diketo acids are potent inhibitors of human immunodeficiency virus (HIV) integrase (IN). Mutations in IN, T66I, S153Y, and M154I, as well as T66I-S153Y and T66I-M154I double mutations, confer resistance to diketo acids (D. J. Hazuda et al., Science 287:646-650, 2000). The effects of these IN mutations on viral replication, enzymatic activity, and susceptibility to other HIV inhibitors are r...
متن کاملStructural and thermodynamic basis of amprenavir/darunavir and atazanavir resistance in HIV-1 protease with mutations at residue 50.
Drug resistance occurs through a series of subtle changes that maintain substrate recognition but no longer permit inhibitor binding. In HIV-1 protease, mutations at I50 are associated with such subtle changes that confer differential resistance to specific inhibitors. Residue I50 is located at the protease flap tips, closing the active site upon ligand binding. Under selective drug pressure, I...
متن کاملMultidimensional QSAR Modeling of Amprenavir Derivatives as HIV-Protease Inhibitors
A computational study has been performed on a series of 55 compounds having (S)-N-(3-(N-(cyclopen-tylmethyl) substituted-phenylsulfonamido)-2-hydroxypropyl) acetamide backbone as HIV-1 protease inhibitors. Various combinations of these specific inhibitors fragments were formed by breaking them at central alicyclic single bonds, while retaining the core. Standard Topomer 3D models were automatic...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 2009
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.02539-08