tetano
Editor, Senior Moderator
Protein Sci
. 2020 Aug 21.
doi: 10.1002/pro.3936. Online ahead of print.
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
Angelo Toto[SUP] 1 [/SUP], Sana Ma[SUP] 2 [/SUP], Francesca Malagrin?[SUP] 1 [/SUP], Lorenzo Visconti[SUP] 1 [/SUP], Livia Pagano[SUP] 1 [/SUP], Kristian Stromgaard[SUP] 2 [/SUP], Stefano Gianni[SUP] 1 [/SUP]
Affiliations
Abstract
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. This article is protected by copyright. All rights reserved.
Keywords: Binding; Envelope protein; Kinetics; PALS1; PDZ; SARS-CoV-2.
. 2020 Aug 21.
doi: 10.1002/pro.3936. Online ahead of print.
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
Angelo Toto[SUP] 1 [/SUP], Sana Ma[SUP] 2 [/SUP], Francesca Malagrin?[SUP] 1 [/SUP], Lorenzo Visconti[SUP] 1 [/SUP], Livia Pagano[SUP] 1 [/SUP], Kristian Stromgaard[SUP] 2 [/SUP], Stefano Gianni[SUP] 1 [/SUP]
Affiliations
- PMID: 32822073
- DOI: 10.1002/pro.3936
Abstract
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. This article is protected by copyright. All rights reserved.
Keywords: Binding; Envelope protein; Kinetics; PALS1; PDZ; SARS-CoV-2.