Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease?

ABSTRACT: The C-terminal domain of SARS-CoV main protease (M^pro-C) can form 3D domain-swapped dimer by exchanging the α₁-helices fully buried inside the protein hydrophobic core, under non-denaturing conditions. Here, we report that M^pro-C can also form amyloid fibrils under the 3D domain-swappable conditions in vitro, and the fibrils are not formed through runaway/propagated domain swapping. It is found that there are positive correlations between the rates of domain swapping dimerization and amyloid fibrillation at different temperatures, and for different mutants. However, some M^pro-C mutants incapable of 3D domain swapping can still form amyloid fibrils, indicating that 3D domain swapping is not essential for amyloid fibrillation. Furthermore, NMR H/D

SUBMITTER: Yuan Z 

PROVIDER: S-EPMC8694786 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature