Your browser doesn't support javascript.
Dual ELISA using SARS-CoV-2 nucleocapsid protein produced in E. coli and CHO cells reveals epitope masking by N-glycosylation.
Rump, Airi; Risti, Robert; Kristal, Mai-Ly; Reut, Jekaterina; Syritski, Vitali; Lookene, Aivar; Ruutel Boudinot, Sirje.
  • Rump A; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, 12618, Estonia. Electronic address: airirump1@gmail.com.
  • Risti R; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, 12618, Estonia. Electronic address: robert.risti@taltech.ee.
  • Kristal ML; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, 12618, Estonia. Electronic address: mlykristal@gmail.com.
  • Reut J; Department of Materials and Environmental Technology, Tallinn University of Technology, Tallinn, 12618, Estonia. Electronic address: jekaterina.reut@taltech.ee.
  • Syritski V; Department of Materials and Environmental Technology, Tallinn University of Technology, Tallinn, 12618, Estonia. Electronic address: vitali.syritski@taltech.ee.
  • Lookene A; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, 12618, Estonia. Electronic address: aivar.lookene@taltech.ee.
  • Ruutel Boudinot S; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, 12618, Estonia. Electronic address: sirje.boudinot@gmail.com.
Biochem Biophys Res Commun ; 534: 457-460, 2021 01 01.
Article in English | MEDLINE | ID: covidwho-1064870
ABSTRACT
Spike and nucleocapsid proteins of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2-SP, SARS-CoV-2-NP) are the main immunogenic targets for antibodies. We herein demonstrate that the glycosylation of SARS-CoV-2-NP masks some of its antibody epitopes. In many cases, this can lead to false-negative serological tests. Deglycosylation of SARS-CoV-2-NP significantly increased the number of positive tests. The glycosylation pattern analysis of this protein revealed that the putative N-linked glycosylation sites, at the amino acid positions 48 and 270, co-located with two of the main immunodominant B cell epitopes.
Subject(s)
Keywords
Fulltext
Print
XML
PubMed Links
Search on Google

Full text: Available Collection: International databases Database: MEDLINE Main subject: Recombinant Proteins / Enzyme-Linked Immunosorbent Assay / Spike Glycoprotein, Coronavirus / Epitopes Limits: Animals / Humans Language: English Journal: Biochem Biophys Res Commun Year: 2021 Document Type: Article

Similar

MEDLINE
LILACS
LIS
Fulltext
Print
XML
PubMed Links
Search on Google

Full text: Available Collection: International databases Database: MEDLINE Main subject: Recombinant Proteins / Enzyme-Linked Immunosorbent Assay / Spike Glycoprotein, Coronavirus / Epitopes Limits: Animals / Humans Language: English Journal: Biochem Biophys Res Commun Year: 2021 Document Type: Article