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SARS-CoV-2 hijacks p38β/MAPK11 to promote viral protein translation
Christina A Higgins; Benjamin E Nilsson-Payant; Andrew Kurland; Chengjin Ye; Tomer M Yaron; Jared L Johnson; Boris Bonaventure; Prithy Adhikary; Ilona Golynker; Brad R Rosenberg; Oded Danziger; Maryline Panis; Lewis C Cantley; Luis Martinez-Sobrido; Benjamin R tenOever; Jeffrey R Johnson.
Afiliación
  • Christina A Higgins; Icahn School of Medicine at Mount Sinai
  • Benjamin E Nilsson-Payant; Icahn School of Medicine at Mount Sinai
  • Andrew Kurland; Icahn School of Medicine at Mount Sinai
  • Chengjin Ye; Texas Biomedical Research Institute
  • Tomer M Yaron; Weill Cornell Medicine
  • Jared L Johnson; Weill Cornell Medicine
  • Boris Bonaventure; Icahn School of Medicine at Mount Sinai
  • Prithy Adhikary; Icahn School of Medicine at Mount Sinai
  • Ilona Golynker; Icahn School of Medicine at Mount Sinai
  • Brad R Rosenberg; Icahn School of Medicine at Mount Sinai
  • Oded Danziger; Icahn School of Medicine at Mount Sinai
  • Maryline Panis; Icahn School of Medicine at Mount Sinai
  • Lewis C Cantley; Weill Cornell Medicine
  • Luis Martinez-Sobrido; Texas Biomedical Research Institute
  • Benjamin R tenOever; Icahn School of Medicine at Mount Sinai
  • Jeffrey R Johnson; Icahn School of Medicine at Mount Sinai
Preprint en En | PREPRINT-BIORXIV | ID: ppbiorxiv-457146
ABSTRACT
SARS-CoV-2, the causative agent of the COVID-19 pandemic, drastically modifies infected cells in an effort to optimize virus replication. Included is the activation of the host p38 mitogen-activated protein kinase (MAPK) pathway, which plays a major role in inflammation and is a central driver of COVID-19 clinical presentations. Inhibition of p38/MAPK activity in SARS-CoV-2-infected cells reduces both cytokine production and viral replication. Here, we combined genetic screening with quantitative phosphoproteomics to better understand interactions between the p38/MAPK pathway and SARS-CoV-2. We found that several components of the p38/MAPK pathway impacted SARS-CoV-2 replication and that p38{beta} is a critical host factor for virus replication, and it prevents activation of the type-I interferon pathway. Quantitative phosphoproteomics uncovered several SARS-CoV-2 nucleocapsid phosphorylation sites near the N-terminus that were sensitive to p38 inhibition. Similar to p38{beta} depletion, mutation of these nucleocapsid residues was associated with reduced virus replication and increased activation of type-I interferon signaling. Taken together, this study reveals a unique proviral function for p38{beta} that is not shared with p38 and supports exploring p38{beta} inhibitor development as a strategy towards developing a new class of COVID-19 therapies. ImportanceSARS-CoV-2 is the causative agent of the COVID-19 pandemic that has claimed millions of lives since its emergence in 2019. SARS-CoV-2 infection of human cells requires the activity of several cellular pathways for successful replication. One such pathway, the p38 mitogen-activated protein kinase (MAPK) pathway, is required for virus replication and disease pathogenesis. Here, we applied systems biology approaches to understand how MAPK pathways benefit SARS-CoV-2 replication to inform the development of novel COVID-19 drug therapies.
Licencia
cc_by_nc_nd
Texto completo: 1 Colección: 09-preprints Base de datos: PREPRINT-BIORXIV Tipo de estudio: Prognostic_studies Idioma: En Año: 2021 Tipo del documento: Preprint
Texto completo: 1 Colección: 09-preprints Base de datos: PREPRINT-BIORXIV Tipo de estudio: Prognostic_studies Idioma: En Año: 2021 Tipo del documento: Preprint