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
| Autor: | Toto A., Ma S., Malagrino Francesca., Visconti L., Pagano L., Stromgaard K., Gianni S. |
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| Přispěvatelé: | Toto, A., Ma, S., Malagrino, Francesca., Visconti, L., Pagano, L., Stromgaard, K., Gianni, S. |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular PDZ Domain binding SARS Viru Betacoronaviru Pandemic PALS1 SARS-CoV-2 Coronavirus Infection Pneumonia Viral kinetic Binding Site COVID-19 Severe Acute Respiratory Syndrome envelope protein Viral Envelope Proteins Peptide PDZ Coronavirus Envelope Protein Amino Acid Sequence Nucleoside-Phosphate Kinase Membrane Protein Human Protein Binding |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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