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10.1101/sqb.2013.78.020339

http://scihub22266oqcxt.onion/10.1101/sqb.2013.78.020339
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suck abstract from ncbi


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pmid24733380
      Cold+Spring+Harb+Symp+Quant+Biol 2013 ; 78 (ä): 81-90
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  • The "histone mimicry" by pathogens #MMPMID24733380
  • Schaefer U ; Ho JS ; Prinjha RK ; Tarakhovsky A
  • Cold Spring Harb Symp Quant Biol 2013[]; 78 (ä): 81-90 PMID24733380 show ga
  • One of the defining characteristics of human and animal viruses is their ability to suppress host antiviral responses. Viruses express proteins that impair the detection of viral nucleic acids by host pattern-recognition receptors, block signaling pathways that lead to the synthesis of type I interferons and other cytokines, or prevent the activation of virus-induced genes. We have identified a novel mechanism of virus-mediated suppression of antiviral gene expression that relies on the presence of histone-like sequences (histone mimics) in viral proteins. We describe how viral histone mimics can interfere with key regulators of gene expression and contribute to the suppression of antiviral responses. We also describe how viral histone mimics can facilitate the identification of novel mechanisms of antiviral gene regulation and lead to the development of drugs that use histone mimicry for interference with gene expression during diseases.
  • |Amino Acid Sequence [MESH]
  • |Animals [MESH]
  • |Antiviral Agents/pharmacology [MESH]
  • |Gene Expression Profiling [MESH]
  • |Gene Expression Regulation [MESH]
  • |Gene Expression Regulation, Viral [MESH]
  • |Histones/*metabolism [MESH]
  • |Host-Pathogen Interactions [MESH]
  • |Humans [MESH]
  • |Influenza A virus/genetics [MESH]
  • |Molecular Sequence Data [MESH]
  • |Protein Structure, Tertiary [MESH]
  • |Transcription, Genetic [MESH]
  • |Viral Nonstructural Proteins/genetics [MESH]
  • |Viral Proteins/*metabolism [MESH]
  • |Virus Diseases/*metabolism [MESH]


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