DING proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of HIV-1 LTR promoter.
Independent research groups reported that DING protein homologues isolated from bacterial, plant and human cells demonstrate the anti-HIV-1 activity. This might indicate that diverse organisms utilize a DING-mediated broad-range protective innate immunity response to pathogen invasion, and that this...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3735540?pdf=render |
| _version_ | 1818193293366788096 |
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| author | Rakhee Sachdeva Nune Darbinian Kamel Khalili Shohreh Amini Daniel Gonzalez Ahmed Djeghader Eric Chabriére Andrew Suh Ken Scott Malgorzata Simm |
| author_facet | Rakhee Sachdeva Nune Darbinian Kamel Khalili Shohreh Amini Daniel Gonzalez Ahmed Djeghader Eric Chabriére Andrew Suh Ken Scott Malgorzata Simm |
| author_sort | Rakhee Sachdeva |
| collection | DOAJ |
| description | Independent research groups reported that DING protein homologues isolated from bacterial, plant and human cells demonstrate the anti-HIV-1 activity. This might indicate that diverse organisms utilize a DING-mediated broad-range protective innate immunity response to pathogen invasion, and that this mechanism is effective also against HIV-1. We performed structural analyses and evaluated the anti-HIV-1 activity for four DING protein homologues isolated from different species. Our data show that bacterial PfluDING, plant p38SJ (pDING), human phosphate binding protein (HPBP) and human extracellular DING from CD4 T cells (X-DING-CD4) share high degrees of structure and sequence homology. According to earlier reports on the anti-HIV-1 activity of pDING and X-DING-CD4, other members of this protein family from bacteria and humans were able to block transcription of HIV-1 and replication of virus in cell based assays. The efficacy studies for DING-mediated HIV-1 LTR and HIV-1 replication blocking activity showed that the LTR transcription inhibitory concentration 50 (IC50) values ranged from 0.052-0.449 ng/ml; and the HIV-1 replication IC50 values ranged from 0.075-0.311 ng/ml. Treatment of cells with DING protein alters the interaction between p65-NF-κB and HIV-1 LTR. Our data suggest that DING proteins may be part of an innate immunity defense against pathogen invasion; the conserved structure and activity makes them appealing candidates for development of a novel therapeutics targeting HIV-1 transcription. |
| first_indexed | 2024-12-12T00:44:06Z |
| format | Article |
| id | doaj.art-e5564c10024e4c07bc8e945016224de9 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-12T00:44:06Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-e5564c10024e4c07bc8e945016224de92022-12-22T00:44:10ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0188e6962310.1371/journal.pone.0069623DING proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of HIV-1 LTR promoter.Rakhee SachdevaNune DarbinianKamel KhaliliShohreh AminiDaniel GonzalezAhmed DjeghaderEric ChabriéreAndrew SuhKen ScottMalgorzata SimmIndependent research groups reported that DING protein homologues isolated from bacterial, plant and human cells demonstrate the anti-HIV-1 activity. This might indicate that diverse organisms utilize a DING-mediated broad-range protective innate immunity response to pathogen invasion, and that this mechanism is effective also against HIV-1. We performed structural analyses and evaluated the anti-HIV-1 activity for four DING protein homologues isolated from different species. Our data show that bacterial PfluDING, plant p38SJ (pDING), human phosphate binding protein (HPBP) and human extracellular DING from CD4 T cells (X-DING-CD4) share high degrees of structure and sequence homology. According to earlier reports on the anti-HIV-1 activity of pDING and X-DING-CD4, other members of this protein family from bacteria and humans were able to block transcription of HIV-1 and replication of virus in cell based assays. The efficacy studies for DING-mediated HIV-1 LTR and HIV-1 replication blocking activity showed that the LTR transcription inhibitory concentration 50 (IC50) values ranged from 0.052-0.449 ng/ml; and the HIV-1 replication IC50 values ranged from 0.075-0.311 ng/ml. Treatment of cells with DING protein alters the interaction between p65-NF-κB and HIV-1 LTR. Our data suggest that DING proteins may be part of an innate immunity defense against pathogen invasion; the conserved structure and activity makes them appealing candidates for development of a novel therapeutics targeting HIV-1 transcription.http://europepmc.org/articles/PMC3735540?pdf=render |
| spellingShingle | Rakhee Sachdeva Nune Darbinian Kamel Khalili Shohreh Amini Daniel Gonzalez Ahmed Djeghader Eric Chabriére Andrew Suh Ken Scott Malgorzata Simm DING proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of HIV-1 LTR promoter. PLoS ONE |
| title | DING proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of HIV-1 LTR promoter. |
| title_full | DING proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of HIV-1 LTR promoter. |
| title_fullStr | DING proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of HIV-1 LTR promoter. |
| title_full_unstemmed | DING proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of HIV-1 LTR promoter. |
| title_short | DING proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of HIV-1 LTR promoter. |
| title_sort | ding proteins from phylogenetically different species share high degrees of sequence and structure homology and block transcription of hiv 1 ltr promoter |
| url | http://europepmc.org/articles/PMC3735540?pdf=render |
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