Comparing the binding properties of peptides mimicking the Envelope protein of SARS-CoV and SARS-CoV-2 to the PDZ domain of the tight junction-associated PALS1 protein
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The Envelope protein (E) is one of the four structural proteins encoded by the genome of SARS-CoV and SARS-CoV-2 Coronaviruses. It is an integral membrane protein, highly expressed in the host cell, which is known to have an important role in Coronaviruses maturation, assembly and virulence. The E protein presents a PDZ-binding motif at its C-terminus. One of the key interactors of the E protein in the intracellular environment is the PDZ containing protein PALS1. This interaction is known to play a key role in the SARS-CoV pathology and suspected to affect the integrity of the lung epithelia. In this paper we measured and compared the affinity of peptides mimicking the E protein from SARS-CoV and SARS-CoV-2 for the PDZ domain of PALS1, through equilibrium and kinetic binding experiments. Our results support the hypothesis that the increased virulence of SARS-CoV-2 compared to SARS-CoV may rely on the increased affinity of its Envelope protein for PALS1.
Original language | English |
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Journal | Protein Science |
Volume | 29 |
Issue number | 10 |
Pages (from-to) | 2038-2042 |
Number of pages | 5 |
ISSN | 0961-8368 |
DOIs | |
Publication status | Published - 2020 |
Bibliographical note
© 2020 The Protein Society.
Links
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7461438/pdf/PRO-29-2038.pdf
Final published version
ID: 249062244