Literature collection of the CovAmInf workgroup.
Editors Joshua T. Berryman Abdul Mannan Baig Artemi Bendandi Daniel Bonhenry Mattheos A.G. Koffas
Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes (2023)
Taniya Bhardwaj, Kundlik Gadhave, Shivani K. Kapuganti, Prateek Kumar, Zacharias Faidon Brotzakis, Kumar Udit Saumya, Namyashree Nayak, Ankur Kumar, Richa Joshi, Bodhidipra Mukherjee, Aparna Bhardwaj, Krishan Gopal Thakur, Neha Garg, Michele Vendruscolo, Rajanish Giri
PubMed: 36806058 DOI: 10.1038/s41467-023-36234-4
Amyloidogenic peptides are abundant in both the SARS-CoV and SARS-CoV-2 proteomes. As an extension of earlier work (Charnley 2022), this study identifies a mechanism by which the virus could trigger amyloidosis. The authors went on to demonstrate the cytotoxicity of NSP11 aggregates. It is worth noting that Nidovirales, and its member family coronaviridae, have the most abundant prion-like domain containing species compared to other eukaryotic viruses (https://doi.org/10.1038/s41598-018-27256-w).
The link you added (Tetz and Tetz) is a very interesting piece that I hadn't seen. Not surprised that nidovirales are tops for prion-like sequences, the "nested" structure of the genome, with multiple ORF, puts an information-content restriction on what can be encoded. Very interested to see that herpesviridae, also associated with amyloid disease, come in second for prion-like sequence content after the nidovirales.