Bhardwaj, Taniya and Gadhave, Kundlik and Kapuganti, Shivani K and Kumar, Prateek and Brotzakis, Z.F and Saumya, Kumar Udit and Nayak, Namyashree and Kumar, Ankur and Joshi , Richa and Mukherjee, Bodhidipra and Bhardwaj, Aparna and Thakur, Krishan Gopal and Garg, Neha and Vendruscolo, Michele and Giri, Rajanish (2023) Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes. Nature communications, 14 (1). ISSN 2041-1723
Full text not available from this repository. (Request a copy)Abstract
The phenomenon of protein aggregation is associated with a wide range of human diseases. Our knowledge of the aggregation behaviour of viral proteins, however, is still rather limited. Here, we investigated this behaviour in the SARS-CoV and SARS-CoV-2 proteomes. An initial analysis using a panel of sequence-based predictors suggested the presence of multiple aggregation-prone regions (APRs) in these proteomes and revealed a strong aggregation propensity in some SARS-CoV-2 proteins. We then studied the in vitro aggregation of predicted aggregation-prone SARS-CoV and SARS-CoV-2 proteins and protein regions, including the signal sequence peptide and fusion peptides 1 and 2 of the spike protein, a peptide from the NSP6 protein, and the ORF10 and NSP11 proteins. Our results show that these peptides and proteins can form amyloid aggregates. We used circular dichroism spectroscopy to reveal the presence of β-sheet rich cores in aggregates and X-ray diffraction and Raman spectroscopy to confirm the formation of amyloid structures. Furthermore, we demonstrated that SARS-CoV-2 NSP11 aggregates are toxic to mammalian cell cultures. These results motivate further studies about the possible role of aggregation of SARS proteins in protein misfolding diseases and other human conditions.
| Item Type: | Article |
|---|---|
| Additional Information: | The copyright of this article belongs to Nature Pub. Group |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 16 Jul 2024 02:27 |
| Last Modified: | 16 Jul 2024 02:27 |
| URI: | http://crdd.osdd.net/open/id/eprint/3166 |
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