In memory of my beautiful sister Elizabeth, mid 40’s.
Thank you. I don’t mind the red text.
https://www.preprints.org/manuscript/202003.0422/v1
https://www.preprints.org/
SARS-CoV-2 Prion-Like Domains in Spike Proteins Enable Higher Affinity to ACE2
George Tetz * ORCID logo and Victor Tetz ORCID logo
Version 1 : Received: 27 March 2020 / Approved: 29 March 2020 / Online: 29 March 2020 (06:16:20 CEST)
A peer-reviewed article of this Preprint also exists.
Tetz, G.; Tetz, V. Prion-like Domains in Spike Protein of SARS-CoV-2 Differ across Its Variants and Enable Changes in Affinity to ACE2. Microorganisms 2022, 10, 280. https://doi.org/10.3390/microorganisms10020280 Tetz, G.; Tetz, V. Prion-like Domains in Spike Protein of SARS-CoV-2 Differ across Its Variants and Enable Changes in Affinity to ACE2. Microorganisms 2022, 10, 280. https://doi.org/10.3390/microorganisms10020280
Journal reference: Microorganisms 2022
DOI: 10.3390/microorganisms10020280
Abstract
Currently, the world is struggling with the coronavirus disease 2019 (COVID-19) pandemic, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Prion-like domains are critical for virulence and the development of therapeutic targets; however, the prion-like domains in the SARS-CoV-2 proteome have not been analyzed. In this in silico study, using the PLAAC algorithm, we identified the presence of prion-like domains in the SARS-CoV-2 spike protein. Compared with other viruses, a striking difference was observed in the distribution of prion-like domains in the spike protein, since SARS-CoV-2 was the only coronavirus with a prion-like domain found in the receptor-binding domain of the S1 region of the spike protein. The presence and unique distribution of prion-like domains in the SARS-CoV-2 receptor-binding domains of the spike protein is particularly interesting, since although the SARS-CoV-2 and SARS-CoV S proteins share the same host cell receptor, angiotensin-converting enzyme 2 (ACE2), SARS-CoV-2 demonstrates a 10- to 20-fold higher affinity for ACE2. Finally, we identified prion-like domains in the α1 helix of the ACE2 receptor that interact with the viral receptor-binding domain of SARS-CoV-2. Taken together, the present findings indicate that the identified PrDs in the SARS-CoV-2 receptor-binding domain (RBD) and ACE2 region that interact with RBD have important functional roles in viral adhesion and entry.
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