Expression and frameshifting but extremely inefficient proteolytic processing of the HIV-1 gag and pol gene products in stably transfected rodent cell lines
Identifieur interne : 001B80 ( Main/Exploration ); précédent : 001B79; suivant : 001B81Expression and frameshifting but extremely inefficient proteolytic processing of the HIV-1 gag and pol gene products in stably transfected rodent cell lines
Auteurs : Dieter Moosmayer [Royaume-Uni] ; Heide Reil [Royaume-Uni] ; Martina Ausmeier [Royaume-Uni] ; Jens-Gerd Scharf [Royaume-Uni] ; Hansjorg Hauser [Royaume-Uni] ; Klaus Dieter Jentsch [Royaume-Uni] ; Gerhard Hunsmann [Royaume-Uni]Source :
- Virology [ 0042-6822 ] ; 1991.
English descriptors
- Teeft :
- Acad, Active luciferase, Aids virus, Cell lines, Cells transfected, Cellular background, Encoding, Frameshift, Frameshifting, Frameshifting efficiency, Fusion protein, Gene, Gene products, Grice, Human immunodeficiency virus, Human immunodeficiency virus type, Human immunodeficiencyvirus, Immunoblot, Immunoblot analysis, Immunoblotting reaction, Immunodeficiency, Insect cells, Jacks, Lmmunoblot, Lmmunoblot analysis, Luciferase, Luciferase activity, Mammalian cells, Mous, Nucleotide, Nucleotide position, Plasmid, Pmpsv, Polyprotein, Precursor, Precursor protein, Primary translation products, Primate, Primate cell lines, Primate cells, Protease, Protease activity, Proteolytic, Proteolytic activity, Proteolytic processing, Rabbit hyperimmune sera, Recombinant, Recombinant protein, Recombinant proteins, Replication, Retroviral, Ribosomal, Ribosomal frameshift, Ribosomal frameshifting, Rodent, Rodent cells, Shifty, Shifty sequence, Soluble fraction, Stable transfectants, Stably, Transcriptase, Transfectants, Transfected, Transfected cells, Transfected rodent cells, Translational, Viral, Viral protease.
Abstract
Abstract: Expression, ribosomal frameshifting, and proteolytic processing of HIV-1 GAG and POL proteins were investigated in heterologous mammalian cells in order to elucidate the influence of the cellular background on these events. DNA fragments encoded by the gag and pol region were expressed in two rodent cell lines, LTK- and BHK. Both stably transfected cell lines continuously produce recombinant proteins which react with HIV-specific antisera. The GAG precursor and a 39-kDa proteolytic fragment thereof were the major recombinant proteins detected. Expression of the gag-pol region leads to the production of the GAG-POL precursor. Ribosomal frameshifting at the HIV-1 shifty sequence to a typical extent could be positively demonstrated by an enzyme assay. Despite the presence of the viral protease within the GAG-POL precursors, proteolytic processing of the HIV-derived polyproteins was extremely inefficient. The efficiency could not be enhanced by overexpression of the HIV-1 protease encoding region.
Url:
DOI: 10.1016/0042-6822(91)90134-W
Affiliations:
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Le document en format XML
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<term>Active luciferase</term>
<term>Aids virus</term>
<term>Cell lines</term>
<term>Cells transfected</term>
<term>Cellular background</term>
<term>Encoding</term>
<term>Frameshift</term>
<term>Frameshifting</term>
<term>Frameshifting efficiency</term>
<term>Fusion protein</term>
<term>Gene</term>
<term>Gene products</term>
<term>Grice</term>
<term>Human immunodeficiency virus</term>
<term>Human immunodeficiency virus type</term>
<term>Human immunodeficiencyvirus</term>
<term>Immunoblot</term>
<term>Immunoblot analysis</term>
<term>Immunoblotting reaction</term>
<term>Immunodeficiency</term>
<term>Insect cells</term>
<term>Jacks</term>
<term>Lmmunoblot</term>
<term>Lmmunoblot analysis</term>
<term>Luciferase</term>
<term>Luciferase activity</term>
<term>Mammalian cells</term>
<term>Mous</term>
<term>Nucleotide</term>
<term>Nucleotide position</term>
<term>Plasmid</term>
<term>Pmpsv</term>
<term>Polyprotein</term>
<term>Precursor</term>
<term>Precursor protein</term>
<term>Primary translation products</term>
<term>Primate</term>
<term>Primate cell lines</term>
<term>Primate cells</term>
<term>Protease</term>
<term>Protease activity</term>
<term>Proteolytic</term>
<term>Proteolytic activity</term>
<term>Proteolytic processing</term>
<term>Rabbit hyperimmune sera</term>
<term>Recombinant</term>
<term>Recombinant protein</term>
<term>Recombinant proteins</term>
<term>Replication</term>
<term>Retroviral</term>
<term>Ribosomal</term>
<term>Ribosomal frameshift</term>
<term>Ribosomal frameshifting</term>
<term>Rodent</term>
<term>Rodent cells</term>
<term>Shifty</term>
<term>Shifty sequence</term>
<term>Soluble fraction</term>
<term>Stable transfectants</term>
<term>Stably</term>
<term>Transcriptase</term>
<term>Transfectants</term>
<term>Transfected</term>
<term>Transfected cells</term>
<term>Transfected rodent cells</term>
<term>Translational</term>
<term>Viral</term>
<term>Viral protease</term>
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<front><div type="abstract" xml:lang="en">Abstract: Expression, ribosomal frameshifting, and proteolytic processing of HIV-1 GAG and POL proteins were investigated in heterologous mammalian cells in order to elucidate the influence of the cellular background on these events. DNA fragments encoded by the gag and pol region were expressed in two rodent cell lines, LTK- and BHK. Both stably transfected cell lines continuously produce recombinant proteins which react with HIV-specific antisera. The GAG precursor and a 39-kDa proteolytic fragment thereof were the major recombinant proteins detected. Expression of the gag-pol region leads to the production of the GAG-POL precursor. Ribosomal frameshifting at the HIV-1 shifty sequence to a typical extent could be positively demonstrated by an enzyme assay. Despite the presence of the viral protease within the GAG-POL precursors, proteolytic processing of the HIV-derived polyproteins was extremely inefficient. The efficiency could not be enhanced by overexpression of the HIV-1 protease encoding region.</div>
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<name sortKey="Scharf, Jens Gerd" sort="Scharf, Jens Gerd" uniqKey="Scharf J" first="Jens-Gerd" last="Scharf">Jens-Gerd Scharf</name>
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