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Screening and affinity optimization of single domain antibody targeting the SARS-CoV-2 nucleocapsid protein.
- Source :
-
PeerJ [PeerJ] 2024 Aug 30; Vol. 12, pp. e17846. Date of Electronic Publication: 2024 Aug 30 (Print Publication: 2024). - Publication Year :
- 2024
-
Abstract
- The coronavirus disease 2019 (COVID-19) pandemic, which caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), lead to a crisis with devastating disasters to global public economy and health. Several studies suggest that the SARS-CoV-2 nucleocapsid protein (N protein) is one of uppermost structural constituents of SARS-CoV-2 and is relatively conserved which could become a specific diagnostic marker. In this study, eight single domain antibodies recognized the N protein specifically which were named pN01-pN08 were screened using human phage display library. According to multiple sequence alignment and molecular docking analyses, the interaction mechanism between antibody and N protein was predicted. ELISA results indicated pN01-pN08 with high affinity to protein N. To improve their efficacy, two fusion proteins were prepared and their affinity was tested. These finding showed that fusion proteins had higher affinity than single domain antibodies and will be used as diagnosis for the pandemic of SARS-CoV-2.<br />Competing Interests: The authors declare that they have no competing interests.<br /> (© 2024 Yang et al.)
- Subjects :
- Humans
Antibody Affinity
Phosphoproteins immunology
Phosphoproteins chemistry
Enzyme-Linked Immunosorbent Assay methods
Recombinant Fusion Proteins immunology
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Peptide Library
Single-Domain Antibodies immunology
Single-Domain Antibodies chemistry
SARS-CoV-2 immunology
Coronavirus Nucleocapsid Proteins immunology
Coronavirus Nucleocapsid Proteins chemistry
COVID-19 immunology
COVID-19 diagnosis
Molecular Docking Simulation
Antibodies, Viral immunology
Subjects
Details
- Language :
- English
- ISSN :
- 2167-8359
- Volume :
- 12
- Database :
- MEDLINE
- Journal :
- PeerJ
- Publication Type :
- Academic Journal
- Accession number :
- 39224822
- Full Text :
- https://doi.org/10.7717/peerj.17846