Abstract
The mitochondrial antiviral signalling protein (MAVS) is a central signal transduction hub in the innate immune response against viral infections. Viral RNA present in the cytoplasm is detected by retinoic acid inducible gene I like receptors, which then activate MAVS via heterotypic interactions between their respective caspase activation and recruitment domains (CARD). This leads to the formation of active, high molecular weight MAVS complexes formed by homotypic interactions between the single N-terminal CARDs of MAVS. Filaments formed by the N-terminal MAVSCARD alone are sufficient to induce the autocatalytic conversion from a monomeric to an aggregated state in a prion-like manner. Here, we present the nearly complete spectroscopic 13C and 15N resonance assignments of human MAVSCARD filaments obtained from a single sample by magic angle spinning solid-state NMR spectroscopy. The corresponding secondary chemical shifts suggest that the filamentous form of MAVSCARD retains an exclusively alpha-helical fold that is very similar to the X-ray structure determined previously from monomeric MAVSCARD-maltose binding protein fusion constructs.
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Acknowledgments
We are grateful to Dr. Mumdooh Ahmed for recording the ssNMR spectra and for helpful discussions. L. H. has been supported by a fellowship from the HZI graduate school.
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He, L., Lührs, T. & Ritter, C. Solid-state NMR resonance assignments of the filament-forming CARD domain of the innate immunity signaling protein MAVS. Biomol NMR Assign 9, 223–227 (2015). https://doi.org/10.1007/s12104-014-9579-6
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DOI: https://doi.org/10.1007/s12104-014-9579-6