Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin.


Journal

bioRxiv : the preprint server for biology
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187

Informations de publication

Date de publication:
19 Jan 2023
Historique:
pubmed: 14 5 2022
medline: 14 5 2022
entrez: 13 5 2022
Statut: epublish

Résumé

The Papain-like protease (PLpro) is a domain of a multi-functional, non-structural protein 3 of coronaviruses. PLpro cleaves viral polyproteins and posttranslational conjugates with poly-ubiquitin and protective ISG15, composed of two ubiquitin-like (UBL) domains. Across coronaviruses, PLpro showed divergent selectivity for recognition and cleavage of posttranslational conjugates despite sequence conservation. We show that SARS-CoV-2 PLpro binds human ISG15 and K48-linked di-ubiquitin (K48-Ub

Identifiants

pubmed: 35547846
doi: 10.1101/2021.09.15.460543
pmc: PMC9094096
pii:
doi:

Types de publication

Preprint

Langues

eng

Commentaires et corrections

Type : UpdateIn

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Auteurs

Pawel M Wydorski (PM)

Molecular Biophysics Graduate Program, University of Texas Southwestern Medical Center, Dallas, TX 75390 USA.
Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390 USA.

Jerzy Osipiuk (J)

Center for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667 USA.
Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439 USA.

Benjamin T Lanham (BT)

Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742 USA.

Christine Tesar (C)

Center for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667 USA.
Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439 USA.

Michael Endres (M)

Center for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667 USA.
Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439 USA.

Elizabeth Engle (E)

Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742 USA.

Robert Jedrzejczak (R)

Center for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667 USA.
Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439 USA.

Vishruth Mullapudi (V)

Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390 USA.

Karolina Michalska (K)

Center for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667 USA.
Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439 USA.

Krzysztof Fidelis (K)

Protein Structure Prediction Center, Genome and Biomedical Sciences Facilities, University of California, Davis, CA, 95616 USA.

David Fushman (D)

Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742 USA.

Andrzej Joachimiak (A)

Center for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667 USA.
Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439 USA.
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, 60367 USA.

Lukasz A Joachimiak (LA)

Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390 USA.
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390 USA.

Classifications MeSH