Mass spectrometry-based proteomic platforms for better understanding of SARS-CoV-2 induced pathogenesis and potential diagnostic approaches.
Animals
COVID-19
/ diagnosis
Host-Pathogen Interactions
Humans
Mass Spectrometry
/ methods
Protein Interaction Mapping
/ methods
Protein Interaction Maps
Protein Kinases
/ analysis
Protein Processing, Post-Translational
Proteome
/ analysis
Proteomics
/ methods
Receptor, EphA2
/ analysis
SARS-CoV-2
/ physiology
Signal Transduction
COVID-19
biomarkers
comparative proteomics
kinase-substrate signaling
post-translational modifications
targeted proteomics
top-down proteomics
Journal
Proteomics
ISSN: 1615-9861
Titre abrégé: Proteomics
Pays: Germany
ID NLM: 101092707
Informations de publication
Date de publication:
05 2021
05 2021
Historique:
revised:
09
04
2021
received:
09
11
2020
accepted:
12
04
2021
pubmed:
17
4
2021
medline:
26
5
2021
entrez:
16
4
2021
Statut:
ppublish
Résumé
While protein-protein interaction is the first step of the SARS-CoV-2 infection, recent comparative proteomic profiling enabled the identification of over 11,000 protein dynamics, thus providing a comprehensive reflection of the molecular mechanisms underlying the cellular system in response to viral infection. Here we summarize and rationalize the results obtained by various mass spectrometry (MS)-based proteomic approaches applied to the functional characterization of proteins and pathways associated with SARS-CoV-2-mediated infections in humans. Comparative analysis of cell-lines versus tissue samples indicates that our knowledge in proteome profile alternation in response to SARS-CoV-2 infection is still incomplete and the tissue-specific response to SARS-CoV-2 infection can probably not be recapitulated efficiently by in vitro experiments. However, regardless of the viral infection period, sample types, and experimental strategies, a thorough cross-comparison of the recently published proteome, phosphoproteome, and interactome datasets led to the identification of a common set of proteins and kinases associated with PI3K-Akt, EGFR, MAPK, Rap1, and AMPK signaling pathways. Ephrin receptor A2 (EPHA2) was identified by 11 studies including all proteomic platforms, suggesting it as a potential future target for SARS-CoV-2 infection mechanisms and the development of new therapeutic strategies. We further discuss the potentials of future proteomics strategies for identifying prognostic SARS-CoV-2 responsive age-, gender-dependent, tissue-specific protein targets.
Identifiants
pubmed: 33860983
doi: 10.1002/pmic.202000279
pmc: PMC8250252
doi:
Substances chimiques
Proteome
0
Protein Kinases
EC 2.7.-
Receptor, EphA2
EC 2.7.10.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2000279Subventions
Organisme : NIH HHS
ID : R01GM116116
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM123055
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM116116
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL133624
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM133840
Pays : United States
Organisme : NSF
ID : OCE-1634630
Organisme : NIH HHS
ID : R01HL133624
Pays : United States
Organisme : NIH HHS
ID : R01GM133840
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01GM123055
Pays : United States
Informations de copyright
© 2021 Wiley-VCH GmbH.
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