PMC:7094172 / 15213-17853
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7094172","sourcedb":"PMC","sourceid":"7094172","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7094172","text":"The presence of multiple intrinsically disordered regions in the N protein precluded the determination of its structure by X-ray crystallography. Instead, we used rigid body modeling of the SAXS data with the N-terminal domain (NTD; solved in this study) and the C-terminal domains (CTD, PDB ID: 6G13).23 In this way, we obtained structural models for the free N protein and its complex with P3 (Figure 3B,C). Excellent fits were obtained. Representative structural models for the full-length protein without and with P3 are shown in Figure 3D,E, respectively. The free N protein formed a tetramer through CTD with the NTD freely hanging in solution (Figure 3D). The conformation of the solution was consistent with structures previously reported for other CoV N proteins.33 The N-P3 complex formed a compact hexadecamer with a sunburst configuration (Figure 3E). The CTDs formed a central ring and non-native NTD dimers formed “spikes” protruding from the ring. Consistent with ligand-induced aggregation, we observed a “blue shift” in the fluorescence spectrum of the full-length MERS-CoV N protein in the presence of P3 (Figure 3F). The addition of P3 also delayed N protein thermal denaturation and changed the shape of the denaturation curve, further suggesting that large protein aggregates formed in the presence of P3 (Figure 3G). The structure explains how N-NTD dimerization decreased MERS-CoV viability. The N protein packages the viral genome into an RNP complex. Several models for N-CTD dimer assembly have been proposed for the formation of filamentous RNPs.33 All of the proposed interfaces between N-CTD dimers occurred on the side-faces of the CTD cuboid perpendicular to the proposed RNA-binding surface (Figure 3H). Combinatorial use of any region on the side-faces of the CTD dimer cuboid may facilitate manipulation of the RNP length and curvature without obstructing the RNA-binding surface.28,34 However, the SAXS results indicated that N-CTD aggregation occurred on the β-sheet floor of the CTD cuboid. For this reason, the RNA-binding surface of the CTD is occluded by the neighboring CTD on the ring and by the non-native NTD dimer making direct contact with the CTD (Figures 3H and S3). In addition, the CTD cuboids in the aggregation naturally form a topologically closed octamer, leaving no open ends for further addition of CTD cuboids to form a long filamentous RNP. Both the loss of the RNA-binding surface and the inability to incorporate further N protein molecules beyond an octamer may inhibit the formation of the RNP. Therefore, P3 may inhibit MERS-CoV RNP formation by inducing N protein 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