Extensive polymorphisms observed in HIV-1 clade B protease gene using high-density oligonucleotide arrays

Kozal, M. J., Shah, N., Shen, N., Yang, R., Fucini, R., Merigan, T. C., Richman, D. D., Morris, D., Hubbell, E., Chee, M., Gingeras, T. R. (1996) Extensive polymorphisms observed in HIV-1 clade B protease gene using high-density oligonucleotide arrays. Nature Medicine, 2 (7). pp. 753-759. ISSN 10788956 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/8673920
DOI: 10.1038/nm0796-753


Naturally occurring mutations in HIV-1-infected patients have important implications for therapy and the outcome of clinical studies. However, little is known about the prevalence of mutations that confer resistance to HIV-1 protease inhibitors in isolates derived from patients naive for such inhibitors. In the first clinical application of high-density oligonucleotide array sequencing, the sequences of 167 viral isolates from 102 patients have been determined. The DNA sequence of USA HIV-1 clade B proteases was found to be extremely variable and 47.5% of the 99 amino acid positions varied. This level of amino acid diversity is greater than that previously known for all worldwide HIV-1 clades combined (40%). Many of the amino acid changes that are known to contribute to drug resistance occurred as natural polymorphisms in isolates from patients who had never received protease inhibitors.

Item Type: Paper
Uncontrolled Keywords: proteinase proteinase inhibitor article dna polymorphism drug resistance human human immunodeficiency virus 1 human immunodeficiency virus infection major clinical study priority journal protein polymorphism Amino Acid Sequence Base Sequence Drug Resistance Microbial HIV Infections HIV Protease HIV Protease Inhibitors HIV-1 Humans Molecular Sequence Data Oligonucleotides Polymorphism Genetic Human immunodeficiency virus
Subjects: diseases & disorders > viral diseases > HIV
bioinformatics > genomics and proteomics > analysis and processing > microarray gene expression processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression
CSHL Authors:
Communities: CSHL labs > Gingeras lab
Depositing User: CSHL Librarian
Date: 1996
Date Deposited: 13 Mar 2012 15:58
Last Modified: 28 Mar 2014 20:03
Related URLs:
URI: https://repository.cshl.edu/id/eprint/25262

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