author_facet Lesner, Adam
Li, Yuchang
Nitkiewicz, Jadwiga
Li, Guanhua
Kartvelishvili, Alex
Kartvelishvili, Magdalena
Simm, Malgorzata
Lesner, Adam
Li, Yuchang
Nitkiewicz, Jadwiga
Li, Guanhua
Kartvelishvili, Alex
Kartvelishvili, Magdalena
Simm, Malgorzata
author Lesner, Adam
Li, Yuchang
Nitkiewicz, Jadwiga
Li, Guanhua
Kartvelishvili, Alex
Kartvelishvili, Magdalena
Simm, Malgorzata
spellingShingle Lesner, Adam
Li, Yuchang
Nitkiewicz, Jadwiga
Li, Guanhua
Kartvelishvili, Alex
Kartvelishvili, Magdalena
Simm, Malgorzata
The Journal of Immunology
A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
Immunology
Immunology and Allergy
author_sort lesner, adam
spelling Lesner, Adam Li, Yuchang Nitkiewicz, Jadwiga Li, Guanhua Kartvelishvili, Alex Kartvelishvili, Magdalena Simm, Malgorzata 0022-1767 1550-6606 The American Association of Immunologists Immunology Immunology and Allergy http://dx.doi.org/10.4049/jimmunol.175.4.2548 <jats:title>Abstract</jats:title> <jats:p>The identity and activity of several anti-HIV soluble factor(s) secreted by CD8 and CD4 T lymphocytes have been determined; however, some of them still await definition. We have established an HIV-1-resistant, transformed CD4 T cell line that secretes HIV-1 resistance protein(s). Our studies indicate that this protein(s), called HIV-1 resistance factor (HRF), inhibits transcription of the virus by interfering with the activity of NF-κB. In the present report we identified the site at which HRF exerts this inhibition by evaluating a set of discrete events in NF-κB action. We tested the κB oligonucleotide binding activity in nuclei of resistant cells, nuclear translocation and binding to the HIV-1 long terminal repeat of p65 and p50 proteins from susceptible cells after exposure to HRF, and the binding of recombinant p50 to the κB oligonucleotide in vitro as affected by prior or simultaneous exposure to HRF. The results of this experimental schema indicate that HRF interacts with p50 after it enters the nucleus, but before its binding to DNA and that this interaction impedes the formation of an NF-κB-DNA complex required for the promotion of transcription. These findings suggest that HRF mediates a novel innate immune response to virus infection.</jats:p> A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer The Journal of Immunology
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title A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_unstemmed A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_full A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_fullStr A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_full_unstemmed A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_short A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_sort a soluble factor secreted by an hiv-1-resistant cell line blocks transcription through inactivating the dna-binding capacity of the nf-κb p65/p50 dimer
topic Immunology
Immunology and Allergy
url http://dx.doi.org/10.4049/jimmunol.175.4.2548
publishDate 2005
physical 2548-2554
description <jats:title>Abstract</jats:title> <jats:p>The identity and activity of several anti-HIV soluble factor(s) secreted by CD8 and CD4 T lymphocytes have been determined; however, some of them still await definition. We have established an HIV-1-resistant, transformed CD4 T cell line that secretes HIV-1 resistance protein(s). Our studies indicate that this protein(s), called HIV-1 resistance factor (HRF), inhibits transcription of the virus by interfering with the activity of NF-κB. In the present report we identified the site at which HRF exerts this inhibition by evaluating a set of discrete events in NF-κB action. We tested the κB oligonucleotide binding activity in nuclei of resistant cells, nuclear translocation and binding to the HIV-1 long terminal repeat of p65 and p50 proteins from susceptible cells after exposure to HRF, and the binding of recombinant p50 to the κB oligonucleotide in vitro as affected by prior or simultaneous exposure to HRF. The results of this experimental schema indicate that HRF interacts with p50 after it enters the nucleus, but before its binding to DNA and that this interaction impedes the formation of an NF-κB-DNA complex required for the promotion of transcription. These findings suggest that HRF mediates a novel innate immune response to virus infection.</jats:p>
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author Lesner, Adam, Li, Yuchang, Nitkiewicz, Jadwiga, Li, Guanhua, Kartvelishvili, Alex, Kartvelishvili, Magdalena, Simm, Malgorzata
author_facet Lesner, Adam, Li, Yuchang, Nitkiewicz, Jadwiga, Li, Guanhua, Kartvelishvili, Alex, Kartvelishvili, Magdalena, Simm, Malgorzata, Lesner, Adam, Li, Yuchang, Nitkiewicz, Jadwiga, Li, Guanhua, Kartvelishvili, Alex, Kartvelishvili, Magdalena, Simm, Malgorzata
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container_title The Journal of Immunology
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description <jats:title>Abstract</jats:title> <jats:p>The identity and activity of several anti-HIV soluble factor(s) secreted by CD8 and CD4 T lymphocytes have been determined; however, some of them still await definition. We have established an HIV-1-resistant, transformed CD4 T cell line that secretes HIV-1 resistance protein(s). Our studies indicate that this protein(s), called HIV-1 resistance factor (HRF), inhibits transcription of the virus by interfering with the activity of NF-κB. In the present report we identified the site at which HRF exerts this inhibition by evaluating a set of discrete events in NF-κB action. We tested the κB oligonucleotide binding activity in nuclei of resistant cells, nuclear translocation and binding to the HIV-1 long terminal repeat of p65 and p50 proteins from susceptible cells after exposure to HRF, and the binding of recombinant p50 to the κB oligonucleotide in vitro as affected by prior or simultaneous exposure to HRF. The results of this experimental schema indicate that HRF interacts with p50 after it enters the nucleus, but before its binding to DNA and that this interaction impedes the formation of an NF-κB-DNA complex required for the promotion of transcription. These findings suggest that HRF mediates a novel innate immune response to virus infection.</jats:p>
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spelling Lesner, Adam Li, Yuchang Nitkiewicz, Jadwiga Li, Guanhua Kartvelishvili, Alex Kartvelishvili, Magdalena Simm, Malgorzata 0022-1767 1550-6606 The American Association of Immunologists Immunology Immunology and Allergy http://dx.doi.org/10.4049/jimmunol.175.4.2548 <jats:title>Abstract</jats:title> <jats:p>The identity and activity of several anti-HIV soluble factor(s) secreted by CD8 and CD4 T lymphocytes have been determined; however, some of them still await definition. We have established an HIV-1-resistant, transformed CD4 T cell line that secretes HIV-1 resistance protein(s). Our studies indicate that this protein(s), called HIV-1 resistance factor (HRF), inhibits transcription of the virus by interfering with the activity of NF-κB. In the present report we identified the site at which HRF exerts this inhibition by evaluating a set of discrete events in NF-κB action. We tested the κB oligonucleotide binding activity in nuclei of resistant cells, nuclear translocation and binding to the HIV-1 long terminal repeat of p65 and p50 proteins from susceptible cells after exposure to HRF, and the binding of recombinant p50 to the κB oligonucleotide in vitro as affected by prior or simultaneous exposure to HRF. The results of this experimental schema indicate that HRF interacts with p50 after it enters the nucleus, but before its binding to DNA and that this interaction impedes the formation of an NF-κB-DNA complex required for the promotion of transcription. These findings suggest that HRF mediates a novel innate immune response to virus infection.</jats:p> A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer The Journal of Immunology
spellingShingle Lesner, Adam, Li, Yuchang, Nitkiewicz, Jadwiga, Li, Guanhua, Kartvelishvili, Alex, Kartvelishvili, Magdalena, Simm, Malgorzata, The Journal of Immunology, A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer, Immunology, Immunology and Allergy
title A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_full A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_fullStr A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_full_unstemmed A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_short A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
title_sort a soluble factor secreted by an hiv-1-resistant cell line blocks transcription through inactivating the dna-binding capacity of the nf-κb p65/p50 dimer
title_unstemmed A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-κB p65/p50 Dimer
topic Immunology, Immunology and Allergy
url http://dx.doi.org/10.4049/jimmunol.175.4.2548