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The innate immune system responds to infection and tissue damage by activating cytosolic sensory complexes called 'inflammasomes'. Cytosolic DNA is sensed by AIM2-like receptors (ALRs) during bacterial and viral infections and in autoimmune diseases. Subsequently, recruitment of the inflammasome adaptor ASC links ALRs to the activation of caspase-1. A controlled immune response is crucial for maintaining homeostasis, but the regulation of ALR inflammasomes is poorly understood. Here we identified the PYRIN domain (PYD)-only protein POP3, which competes with ASC for recruitment to ALRs, as an inhibitor of DNA virus-induced activation of ALR inflammasomes in vivo. Data obtained with a mouse model with macrophage-specific POP3 expression emphasize the importance of the regulation of ALR inflammasomes in monocytes and macrophages.

Original publication




Journal article


Nat Immunol

Publication Date





343 - 353


Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Carrier Proteins, Caspase 1, DNA Virus Infections, DNA Viruses, DNA-Binding Proteins, HEK293 Cells, Humans, Immunity, Inflammasomes, Interferon Type I, Interferon-gamma, MTOR Associated Protein, LST8 Homolog, Macrophages, Mice, Mice, Inbred C57BL, Mice, Transgenic, Molecular Sequence Data, Multiprotein Complexes, Nuclear Proteins, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Transgenes, Viral Proteins