Both ADP-Ribosyl-Binding and Hydrolase Activities of the Alphavirus nsP3 Macrodomain Affect Neurovirulence in Mice.

Adenosine Diphosphate Ribose / genetics Animals Brain / virology Cell Line Encephalomyelitis / virology Female Hydrolases / genetics Mice Mutation Neurons / virology Signal Transduction Sindbis Virus / genetics Viral Nonstructural Proteins / genetics Virulence Virus Replication / genetics
ADP-ribosyl hydrolase ADP-ribosyl-binding activity Sindbis virus alphavirus antibody encephalomyelitis innate immune response macrodomain nsP3

Journal

mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231

Informations de publication

Date de publication:
11 02 2020
Historique:
entrez: 13 2 2020
pubmed: 13 2 2020
medline: 21 10 2020
Statut: epublish

Résumé

Macrodomain (MD), a highly conserved protein fold present in a subset of plus-strand RNA viruses, binds to and hydrolyzes ADP-ribose (ADPr) from ADP-ribosylated proteins. ADPr-binding by the alphavirus nonstructural protein 3 (nsP3) MD is necessary for the initiation of virus replication in neural cells, whereas hydrolase activity facilitates replication complex amplification. To determine the importance of these activities for pathogenesis of alphavirus encephalomyelitis, mutations were introduced into the nsP3 MD of Sindbis virus (SINV), and the effects on ADPr binding and hydrolase activities, virus replication, immune responses, and disease were assessed. Elimination of ADPr-binding and hydrolase activities (G32E) severely impaired

Identifiants

DOI: 10.1128/mBio.03253-19 PMID: 32047134 PMC: PMC7018654
pubmed: 32047134
pii: mBio.03253-19
doi: 10.1128/mBio.03253-19
pmc: PMC7018654
pii:
doi:

Substances chimiques

Viral Nonstructural Proteins 0
Adenosine Diphosphate Ribose 20762-30-5
Hydrolases EC 3.-

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM104135
Pays : United States
Organisme : NIAID NIH HHS
ID : R56 AI137264
Pays : United States
Organisme : NCI NIH HHS
ID : T32 CA009110
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM080189
Pays : United States

Informations de copyright

Copyright © 2020 Abraham et al.

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Auteurs

Rachy Abraham (R)

W. Harry Feinstone Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.

Robert L McPherson (RL)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.

Morgan Dasovich (M)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.
Department of Chemistry, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, Maryland, USA.

Mohsen Badiee (M)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.

Anthony K L Leung (AKL)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA anthony.leung@jhu.edu dgriffi6@jhu.edu.
Department of Molecular Biology and Genetics, School of Medicine, Johns Hopkins University, Baltimore, Maryland, USA.
Department of Oncology, School of Medicine, Johns Hopkins University, Baltimore, Maryland, USA.

Diane E Griffin (DE)

W. Harry Feinstone Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA anthony.leung@jhu.edu dgriffi6@jhu.edu.

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Classifications MeSH

questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Ribonucléotides › Nucléoside diphosphate ose › Adénosine diphosphate ose › Adénosine diphosphate ribose › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Eucaryotes › Animaux › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Système nerveux › Système nerveux central › Encéphale › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Cellules › Cellules cultivées › Lignée cellulaire › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Maladies du système nerveux › Encéphalomyélite › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Phénomènes génétiques › Variation génétique › Mutation › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Cellules › Neurones › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Transduction du signal › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Virus › Virus à ARN › Virus à ARN à brin positif › Togaviridae › Alphavirus › Virus Sindbis › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines virales non structurales › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Phénomènes microbiologiques › Virulence › Both ADP-Ribosyl-Binding and Hydrolase...
questionsmedicales.fr › Phénomènes microbiologiques › Phénomènes physiologiques viraux › Réplication virale › Both ADP-Ribosyl-Binding and Hydrolase...