Source:http://linkedlifedata.com/resource/pubmed/id/11153080
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
2001-1-19
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pubmed:abstractText |
The human endogenous retrovirus, type K (HERV-K) represents the most biologically active form of known retroelements present in the human genome. Several HERV-K genomes have transcriptionally active open reading frames and encode their own protease (PR). The HERV-K PR has been shown to authentically cleave human immunodeficiency virus type 1 (HIV-1) matrix-capsid peptide in the presence of HIV-1 PR inhibitors. This raised the possibility that HERV-K PR could complement HIV-1 PR function in HIV-1-infected individuals. To investigate this possibility, we fused the HIV-1 vpr gene to the HERV-K PR gene (vpr-PR). The vpr-PR expression plasmid and a PR-defective HIV-1 clone were cotransfected into 293T cells. Progeny virions were assayed for processing of the HIV-1 polyproteins by Western blot and for changes in infectivity. HERV-K PR fused to Vpr was incorporated into HIV-1 virions at a high concentration and cleaved the Gag and Pol precursor proteins. However, neither Gag nor Pol polyproteins were correctly processed. Moreover, the HERV-K PR did not restore virus infectivity. While these results do not exclude the possibility that the HERV-K PR could complement an HIV-1 PR whose function is impaired due to drugs or drug-resistant mutations, they clearly demonstrate that the HERV-K PR cannot substitute for the function of the wild-type HIV-1 PR.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Fusion Proteins, gag-pol,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, vpr,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Protease,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/vpr Gene Products, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0889-2229
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1973-80
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11153080-Cell Line,
pubmed-meshheading:11153080-Endogenous Retroviruses,
pubmed-meshheading:11153080-Endopeptidases,
pubmed-meshheading:11153080-Fusion Proteins, gag-pol,
pubmed-meshheading:11153080-Gene Products, vpr,
pubmed-meshheading:11153080-Genes, vpr,
pubmed-meshheading:11153080-HIV Protease,
pubmed-meshheading:11153080-HIV-1,
pubmed-meshheading:11153080-HeLa Cells,
pubmed-meshheading:11153080-Humans,
pubmed-meshheading:11153080-Plasmids,
pubmed-meshheading:11153080-Protein Precursors,
pubmed-meshheading:11153080-Recombinant Fusion Proteins,
pubmed-meshheading:11153080-Transfection,
pubmed-meshheading:11153080-Virion,
pubmed-meshheading:11153080-vpr Gene Products, Human Immunodeficiency Virus
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pubmed:year |
2000
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pubmed:articleTitle |
Analysis of human immunodeficiency virus type 1 containing HERV-K protease.
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pubmed:affiliation |
Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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