Abstract: Compositions and methods for detecting Toll-like receptor binding to ligands and test compounds are disclosed herein.

Abstract: The invention includes fusion polypeptides including a first fluorescent protein, e.g., a FRET donor protein, a second fluorescent protein, e.g., a FRET acceptor protein, and, linked to at least one of the fluorescent (e.g., FRET donor or FRET acceptor) proteins, an Fc-region of an immunoglobulin. The polypeptide can be immobilized with respect to a surface via the Fc-region even in the absence of antibodies to either the FRET donor protein or FRET acceptor protein, and can be used as a calibration standard for fluorescence resonance energy transfer includes a polypeptide.

Abstract: Provided herein are methods of identifying and using compounds that modulate an AIM2 polypeptide-mediated immune response. Further provided herein are methods of treating disease comprising administering to a patient a compound that decreases expression of an AIM2 polypeptide. Further provided herein are methods of providing gene therapy to a patient comprising administering to the patient a gene therapy agent and a compound that decreases expression of an AIM2 polypeptide. In certain embodiments, a compound that decreases expression of an AIM2 polypeptide comprises an siRNA or an shRNA.

Abstract: Compositions and methods for detecting Toll-like receptor binding to ligands and test compounds are disclosed herein.

Abstract: Methods of identifying compounds that modulate the interaction between a TLR and a molecule that interacts with the TLR by direct binding or by inclusion in a complex that associates with the TLR are described. Methods of identifying molecules that interact with a TLR are also described.

Abstract: TLR9 is localized to endoplasmic reticulum and upon stimulation with a TLR9 ligand, is transported to a tubular lysosomal compartment as is CpG-DNA. Furthermore, it is shown that TLR9 and CpG-DNA directly bind. It was also found that the MyD88 translocates in response to activation of TLR9-mediated signaling. Methods of identifying compounds that affect translocation and activity of TLR9 and MyD88 are described.

Abstract: Methods of treating an inflammatory disorder and inhibiting inflammation by administering an inhibitor of a pH-activated protease are provided.

Abstract: TLR9 is localized to endoplasmic reticulum and upon stimulation with a TLR9 ligand, is transported to a tubular lysosomal compartment as is CpG-DNA. Furthermore, it is shown that TLR9 and CpG-DNA directly bind. It was also found that the MyD88 translocates in response to activation of TLR9-mediated signaling. Methods of identifying compounds that affect translocation and activity of TLR9 and MyD88 are described.

Abstract: Provided herein are methods of identifying and using compounds that modulate an AIM2 polypeptide-mediated immune response. Further provided herein are methods of treating disease comprising administering to a patient a compound that decreases expression of an AIM2 polypeptide. Further provided herein are methods of providing gene therapy to a patient comprising administering to the patient a gene therapy agent and a compound that decreases expression of an AIM2 polypeptide. In certain embodiments, a compound that decreases expression of an AIM2 polypeptide comprises an siRNA or an shRNA.

Abstract: The invention includes fusion polypeptides including a first fluorescent protein, e.g., a FRET donor protein, a second fluorescent protein, e.g., a FRET acceptor protein, and, linked to at least one of the fluorescent (e.g., FRET donor or FRET acceptor) proteins, an Fc-region of an immunoglobulin. The polypeptide can be immobilized with respect to a surface via the Fc-region even in the absence of antibodies to either the FRET donor protein or FRET acceptor protein, and can be used as a calibration standard for fluorescence resonance energy transfer includes a polypeptide.

Abstract: TLR9 is localized to endoplasmic reticulum and upon stimulation with a TLR9 ligand, is transported to a tubular lysosomal compartment as is CpG-DNA. Furthermore, it is shown that TLR9 and CpG-DNA directly bind. It was also found that the MyD88 translocates in response to activation of TLR9-mediated signaling. Methods of identifying compounds that affect translocation and activity of TLR9 and MyD88 are described.

Abstract: Methods of identifying compounds that modulate the interaction between a TLR and a molecule that interacts with the TLR by direct binding or by inclusion in a complex that associates with the TLR are described. Methods of identifying molecules that interact with a TLR are also described.

Abstract: TLR9 is localized to endoplasmic reticulum and upon stimulation with a TLR9 ligand, is transported to a tubular lysosomal compartment as is CpG-DNA. Furthermore, it is shown that TLR9 and CpG-DNA directly bind. It was also found that the MyD88 translocates in response to activation of TLR9-mediated signaling. Methods of identifying compounds that affect translocation and activity of TLR9 and MyD88 are described.

Abstract: Methods of identifying compounds that modulate the interaction between a TLR and a molecule that interacts with the TLR by direct binding or by inclusion in a complex that associates with the TLR are described. Methods of identifying molecules that interact with a TLR are also described.