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  • 标题:Proteomic screening of variola virus reveals a unique NF-κB inhibitor that is highly conserved among pathogenic orthopoxviruses
  • 本地全文:下载
  • 作者:Mohamed R. Mohamed ; Masmudur M. Rahman ; Jerry S. Lanchbury
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2009
  • 卷号:106
  • 期号:22
  • 页码:9045-9050
  • DOI:10.1073/pnas.0900452106
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Identification of the binary interactions between viral and host proteins has become a valuable tool for investigating viral tropism and pathogenesis. Here, we present the first systematic protein interaction screening of the unique variola virus proteome by using yeast 2-hybrid screening against a variety of human cDNA libraries. Several protein-protein interactions were identified, including an interaction between variola G1R, an ankryin/F-box containing protein, and human nuclear factor kappa-B1 (NF-{kappa}B1)/p105. This represents the first direct interaction between a pathogen-encoded protein and NF-{kappa}B1/p105. Orthologs of G1R are present in a variety of pathogenic orthopoxviruses, but not in vaccinia virus, and expression of any one of these viral proteins blocks NF-{kappa}B signaling in human cells. Thus, proteomic screening of variola virus has the potential to uncover modulators of the human innate antiviral responses.
  • 关键词:ankyrin repeats ; Skp1 ; yeast 2-hybrid
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