Host- and pathogen-associated cytoplasmic double-stranded DNA triggers the activation of a NALP3-independent inflammasome, which activates caspase-1, leading to maturation of pro-interleukin-1beta and inflammation. Several studies have isolated AIM2 (absent in melanoma 2) as a candidate cytoplasmic-DNA-sensing protein that contains an N-terminal pyrin domain and C-terminal oligonucleotide binding domain. A screen for transcripts induced by interferon-beta identified AIM2 gene expression. AIM2 protein bound double-stranded DNA, recruited the inflammasome adaptor ASC, and localized to ASC containing speckles. AIM2 and ASC form a pyroptosome, which induces pyroptotic cell death mediated by caspase-1. RNA-mediated suppression of AIM2 expression impairs DNA-induced maturation of interleukin-1beta in THP-1 human monocytic cells, as well as abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus. Thus, AIM2 is a DNA-sensing protein for the activation of the caspase-1 inflammasome.
References
Western blot analysis of human Jurkat cells (lane 1), mouse macrophages untreated (lane 2) and treated (lane 3) with IFNγ (10 ng/ml) and LPS (1µg/ml) for 12 hr (20 µg/lane). The blot was probed with rabbit polyclonal anti-AIM2 (N-terminal region) antibody at 1:1000.
Western blot analysis of human recombinant AIM2 full length sequence with N-terminal GST tag (62 kDa). The blot was probed with rabbit polyclonal anti-AIM2 (N-terminal region) antibody at 1:250 (lane 1) and 1:1000 (lane 2).
*For more information, see UniProt Accession O14862
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blotmobilities of known proteins with similar MW.
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