PXD023016 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Proteomic Investigation Reveals Dominant Alterations of Neutrophil Degranulation and mRNA Translation Pathways in COVID-19 Patients |
Description | The altered molecular proteins and pathways in response to COVID-19 infection are still unclear. Here, we performed a comprehensive proteomics-based investigation of of nasopharyngeal swab samples from COVID-19 patients to identify viral and host peptides by employing simple extraction strategies and also established a panel of host proteins using high-resolution mass spectrometry. The differentially expressed peptides/proteins identified from host and pathogen correlated with the viral load of the host which indicates that these proteins might be good prognostic biomarkers of severity prediction. A few host proteins such as Interleukin-6, L-lactate dehydrogenase, C-reactive protein, Ferritin and Aspartate aminotransferase was found to be upregulated in COVID-19 positive patients using targeted MRM study. Further, the proteins L-lactate dehydrogenase, Aspartate aminotransferase and Alanine aminotransferase was also validated in the clinical settings using immunological assays. We also identified neutrophil degranulation, platelet degranulation, interleukin-12 signaling pathways, mRNA translation of proteins and , co-factor metabolomic process protein metabolism, and stress responses to be key GO enriched pathways, thus altered in the COVID-19 infected patients.providing the detailed investigation of host response in COVID-19 infection , thus providing the landscape of COVID-19 pathophysiology. This study thus also revealed that mass spectrometry-based detected host proteins/peptides has a potential for clinical translation and a few proteins might be routinely monitored in clinics for the disease progression, peptide tests can be used by clinicians for diagnosis as well as identified pathways/ markers as the predictors of disease progression. Furthermore, the identified proteins and their drug binding studies might aid in COVID-19 therapeutic interventions. |
HostingRepository | PRIDE |
AnnounceDate | 2021-02-15 |
AnnouncementXML | Submission_2021-02-14_22:59:38.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Avinash Singh |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monoacetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-12-09 01:35:12 | ID requested | |
⏵ 1 | 2021-02-14 22:59:39 | announced | |
2 | 2023-11-14 08:51:41 | announced | 2023-11-14: Updated project metadata. |
Publication List
Bankar R, Suvarna K, Ghantasala S, Banerjee A, Biswas D, Choudhury M, Palanivel V, Salkar A, Verma A, Singh A, Mukherjee A, Pai MGJ, Roy J, Srivastava A, Badaya A, Agrawal S, Shrivastav O, Shastri J, Srivastava S, Proteomic investigation reveals dominant alterations of neutrophil degranulation and mRNA translation pathways in patients with COVID-19. iScience, 24(3):102135(2021) [pubmed] |
Keyword List
ProteomeXchange project tag: Covid-19 |
submitter keyword: COVID-19, Human, Nasopharyngeal swab, SARS-CoV-2, Mass spectrometry, Proteomics |
Contact List
Sanjeeva Srivastava |
contact affiliation | Proteomics Lab, 304, BSBE Department, Indian Institute Technology Bombay, Powai, Mumbai, India-400076 |
contact email | sanjeeva@iitb.ac.in |
lab head | |
Avinash Singh |
contact affiliation | PhD student |
contact email | singhavi739@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD023016
- Label: PRIDE project
- Name: Proteomic Investigation Reveals Dominant Alterations of Neutrophil Degranulation and mRNA Translation Pathways in COVID-19 Patients