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DING Proteins from Phylogenetically Different Species Share High Degrees of Sequence and Structure Homology and Block Transcription of HIV-1 LTR Promoter

Sachdeva, R
; 
Darbinian, N
; 
Khalili, K
; 
Amini, S
; 
Gonzalez, D
; 
Djeghader, A
; 
Chabriére, E
; 
Suh, A
; 
Scott, K
; 
Simm, M
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Genre
Journal Article
Date
2013-08-06
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Department
Subject
Amino Acid Sequence
 Anti-HIV Agents
 Cell Line, Tumor
 Conserved Sequence
 HIV-1
 Humans
 Hypericum
 Inhibitory Concentration 50
 Models, Molecular
 Molecular Sequence Data
 NF-kappa B p50 Subunit
 Phylogeny
 Polycomb Repressive Complex 1
 Promoter Regions, Genetic
 Protein Multimerization
 Protein Structure, Quaternary
 Pseudomonas fluorescens
 Sequence Homology, Amino Acid
 Terminal Repeat Sequences
 Transcription Factor RelA
 Transcription, Genetic
 Virus Replication
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http://hdl.handle.net/20.500.12613/5385
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DOI
10.1371/journal.pone.0069623
Abstract
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. © 2013 Sachdeva et al.
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