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Variable posttranslational modifications of severe acute respiratory syndrome coronavirus 2 nucleocapsid protein.
| Content Provider | Europe PMC |
|---|---|
| Author | Supekar, Nitin T Shajahan, Asif Gleinich, Anne S Rouhani, Daniel S Heiss, Christian Chapla, Digantkumar Gopaldas Moremen, Kelley W Azadi, Parastoo |
| Copyright Year | 2021 |
| Abstract | AbstractSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which causes coronavirus disease 2019 (COVID-19), started in 2019 in China and quickly spread into a global pandemic. Nucleocapsid protein (N protein) is highly conserved and is the most abundant protein in coronaviruses and is thus a potential target for both vaccine and point-of-care diagnostics. N Protein has been suggested in the literature as having posttranslational modifications (PTMs), and accurately defining these PTMs is critical for its potential use in medicine. Reports of phosphorylation of N protein have failed to provide detailed site-specific information. We have performed comprehensive glycomics, glycoproteomics and proteomics experiments on two different N protein preparations. Both were expressed in HEK293 cells; one was in-house expressed and purified without a signal peptide (SP) sequence, and the other was commercially produced with a SP channeling it through the secretory pathway. Our results show completely different PTMs on the two N protein preparations. The commercial product contained extensive N- and O-linked glycosylation as well as O-phosphorylation on site Thr393. Conversely, the native N Protein model had O-phosphorylation at Ser176 and no glycosylation, highlighting the importance of knowing the provenance of any commercial protein to be used for scientific or clinical studies. Recent studies have indicated that N protein can serve as an important diagnostic marker for COVID-19 and as a major immunogen by priming protective immune responses. Thus, detailed structural characterization of N protein may provide useful insights for understanding the roles of PTMs on viral pathogenesis, vaccine design and development of point-of-care diagnostics. |
| Related Links | https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC8241430&blobtype=pdf |
| Page Count | 13 |
| ISSN | 09596658 |
| Journal | Glycobiology |
| Volume Number | 31 |
| DOI | 10.1093/glycob/cwab044 |
| PubMed Central reference number | PMC8241430 |
| Issue Number | 9 |
| PubMed reference number | 33997890 |
| e-ISSN | 14602423 |
| Language | English |
| Publisher | Oxford University Press |
| Publisher Date | 2021-09-01 |
| Access Restriction | Open |
| Rights License | This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) © The Author(s) 2021. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com |
| Subject Keyword | glycosylation of SARS-CoV-2 N protein N protein phosphorylation N protein site-mapping SARS-CoV-2 nucleocapsid posttranslational modifications SARS-CoV-2 phosphoproteomics |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry |
