SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein

SARS-CoV-2 non-structural protein Nsp14 is a highly conserved enzyme necessary for viral replication. Nsp14 forms a stable complex with non-structural protein Nsp10 and exhibits exoribonuclease and N7-methyltransferase activities. Protein-interactome studies identified human sirtuin 5 (SIRT5) as a p...

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Bibliographic Details
Published in:	PLoS pathogens Vol. 18; no. 9; p. e1010811
Main Authors:	Walter, Marius, Chen, Irene P., Vallejo-Gracia, Albert, Kim, Ik-Jung, Bielska, Olga, Lam, Victor L., Hayashi, Jennifer M., Cruz, Andrew, Shah, Samah, Soveg, Frank W., Gross, John D., Krogan, Nevan J., Jerome, Keith R., Schilling, Birgit, Ott, Melanie, Verdin, Eric
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 01.09.2022 Public Library of Science (PLoS)
Subjects:	Aging Antiviral Agents Antiviral drugs Biology and life sciences Cell culture Coronaviruses COVID-19 Editing Exoribonucleases - metabolism Genomes Health aspects Histones Humans Hypotheses Immune response Infections Innate immunity Lysine Medicine and health sciences Metabolism Methyltransferase Methyltransferases - metabolism Mitochondria NAD Physical Sciences Plasmids Protein turnover Proteins Proviruses Replication Research and Analysis Methods RNA polymerase RNA, Viral - metabolism SARS-CoV-2 Scientific imaging Severe acute respiratory syndrome Severe acute respiratory syndrome coronavirus 2 Sirtuins - genetics Therapeutic applications Transcription factors Viral diseases Viral infections Viral Nonstructural Proteins - metabolism United States
ISSN:	1553-7374, 1553-7366, 1553-7374
Online Access:	Get full text
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