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Mass spectrometry-based proteomic platforms for better understanding of SARS-CoV-2 induced pathogenesis and potential diagnostic approaches.

Abstract
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.
AuthorsNagib Ahsan, R Shyama Prasad Rao, Rashaun S Wilson, Ujwal Punyamurtula, Fernanda Salvato, Max Petersen, Mohammad Kabir Ahmed, M Ruhul Abid, Jacob C Verburgt, Daisuke Kihara, Zhibo Yang, Luca Fornelli, Steven B Foster, Bharat Ramratnam
JournalProteomics (Proteomics) Vol. 21 Issue 10 Pg. e2000279 (05 2021) ISSN: 1615-9861 [Electronic] Germany
PMID33860983 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, U.S. Gov't, Non-P.H.S., Review)
Copyright© 2021 Wiley-VCH GmbH.
Chemical References
  • Proteome
  • Protein Kinases
  • Receptor, EphA2
Topics
  • Animals
  • COVID-19 (diagnosis, metabolism, pathology)
  • Host-Pathogen Interactions
  • Humans
  • Mass Spectrometry (methods)
  • Protein Interaction Mapping (methods)
  • Protein Interaction Maps
  • Protein Kinases (analysis, metabolism)
  • Protein Processing, Post-Translational
  • Proteome (analysis, metabolism)
  • Proteomics (methods)
  • Receptor, EphA2 (analysis, metabolism)
  • SARS-CoV-2 (physiology)
  • Signal Transduction

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