Monoclonal Antibodies to S and N SARS-CoV-2 Proteins as Probes to Assess Structural and Antigenic Properties of Coronaviruses.

Autor: Kumar R; Department of Microbiology & Immunology, Penn State College of Medicine, Hershey, PA 17033, USA., Christensen ND; Department of Pathology, Penn State College of Medicine, Hershey, PA 17033, USA.; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA., Kaddis Maldonado RJ; Department of Medicine, Penn State College of Medicine, Hershey, PA 17033, USA., Bewley MC; Department of Biochemistry & Molecular Biology, Penn State College of Medicine, Hershey, PA 17033, USA., Ostman A; Department of Microbiology & Immunology, Penn State College of Medicine, Hershey, PA 17033, USA., Sudol M; Department of Medicine, Penn State College of Medicine, Hershey, PA 17033, USA., Chen EC; Department of Medicine, Penn State College of Medicine, Hershey, PA 17033, USA., Buchkovich NW; Department of Microbiology & Immunology, Penn State College of Medicine, Hershey, PA 17033, USA., Gontu A; Department of Veterinary and Biomedical Sciences, Penn State University, University Park, PA 16802, USA., Surendran Nair M; Department of Veterinary and Biomedical Sciences, Penn State University, University Park, PA 16802, USA., Nissly RH; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA.; Department of Veterinary and Biomedical Sciences, Penn State University, University Park, PA 16802, USA., Minns AM; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA.; Department of Animal Science, Penn State University, University Park, PA 16802, USA., Kapur V; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA.; Department of Animal Science, Penn State University, University Park, PA 16802, USA., Rossi R; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA., Kuchipudi SV; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA.; Department of Veterinary and Biomedical Sciences, Penn State University, University Park, PA 16802, USA., Lindner SE; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA.; Department of Biochemistry and Molecular Biology, Penn State University, University Park, PA 16802, USA., Parent LJ; Department of Microbiology & Immunology, Penn State College of Medicine, Hershey, PA 17033, USA.; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA.; Department of Medicine, Penn State College of Medicine, Hershey, PA 17033, USA., Flanagan JM; Huck Institutes of the Life Sciences, Penn State University, University Park, PA 16802, USA.; Department of Biochemistry & Molecular Biology, Penn State College of Medicine, Hershey, PA 17033, USA., Buchkovich NJ; Department of Microbiology & Immunology, Penn State College of Medicine, Hershey, PA 17033, USA.
Jazyk: angličtina
Zdroj: Viruses [Viruses] 2021 Sep 22; Vol. 13 (10). Date of Electronic Publication: 2021 Sep 22.
DOI: 10.3390/v13101899
Abstrakt: Antibodies targeting the spike (S) and nucleocapsid (N) proteins of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are essential tools. In addition to important roles in the treatment and diagnosis of infection, the availability of high-quality specific antibodies for the S and N proteins is essential to facilitate basic research of virus replication and in the characterization of mutations responsible for variants of concern. We have developed panels of mouse and rabbit monoclonal antibodies (mAbs) to the SARS-CoV-2 spike receptor-binding domain (S-RBD) and N protein for functional and antigenic analyses. The mAbs to the S-RBD were tested for neutralization of native SARS-CoV-2, with several exhibiting neutralizing activity. The panels of mAbs to the N protein were assessed for cross-reactivity with the SARS-CoV and Middle East respiratory syndrome (MERS)-CoV N proteins and could be subdivided into sets that showed unique specificity for SARS-CoV-2 N protein, cross-reactivity between SARS-CoV-2 and SARS-CoV N proteins only, or cross-reactivity to all three coronavirus N proteins tested. Partial mapping of N-reactive mAbs were conducted using truncated fragments of the SARS-CoV-2 N protein and revealed near complete coverage of the N protein. Collectively, these sets of mouse and rabbit monoclonal antibodies can be used to examine structure/function studies for N proteins and to define the surface location of virus neutralizing epitopes on the RBD of the S protein.
Databáze: MEDLINE