EVALUATION OF INTERACTIONS OF SARS-COV-2 STRUCTURAL PROTEINS WITH SPECIFIC ANTIBODIES BY SPR ASSAY

Authors

  • Petia Genova-Kalou National Centre of Infectious and Parasitic Diseases Author
  • G. Dyankov Institute of Optical Materials and Technologies, Bulgarian Academy of Sciences, Sofia 1113, 109 Acad. G. Bonchev Str., Bulgaria Author
  • H. Kisov Institute of Optical Materials and Technologies, Bulgarian Academy of Sciences, Sofia 1113, 109 Acad. G. Bonchev Str., Bulgaria Author
  • V. Mankov Institute of Optical Materials and Technologies, Bulgarian Academy of Sciences, Sofia 1113, 109 Acad. G. Bonchev Str., Bulgaria Author
  • Evdokiya Hikova Institute of Optical Materials and Technologies, Bulgarian Academy of Sciences, Sofia 1113, 109 Acad. G. Bonchev Str., Bulgaria Author
  • Stefka Krumova National Center of Infectious and Parasitic Diseases, Department of Virology, 44A “Gen. Stoletov” Blvd., 1233 Sofia, Bulgaria Author
  • N. Malinowski Institute of Optical Materials and Technologies, Bulgarian Academy of Sciences, Sofia 1113, 109 Acad. G. Bonchev Str., Bulgaria Author

DOI:

https://doi.org/10.58395/peg69k16

Keywords:

SARS-CoV-2, spike (S-) protein, nucleocapsid (N-) protein, anti-SARS-CoV-1/2 antibodies, Surface Plasmon Resonance (SPR) assay

Abstract

Background: The World Health Organization admitted that the vaccination against Covid 19 limited the deaths, but not the spread of the disease. This requires a method allowing a specific, rapid and accurate diagnosis of the disease. We report a SPR assay that meets the requirements and can be applied no only for SARS Cov-2 diagnosis but as a tool for early diagnosis of otherinfections.

Methods: Surface plasmon resonance (SPR) method was used to identify the binding of S/N protein to monoclonal antibodies. N-protein monoclonal antibody (NP mAb), S-protein monoclonal antibody (SP mAb), and receptor bind domain (RBD) antibody were used as recognition molecules. Ligands were deposited by the matrix-assisted laser evaporation (MAPLE) method, which guarantees maximum interaction specificity.

Results: We registered S/N protein binding to the corresponding mAbs and S protein to RBD antibody with high sensitivity: the interactions were observed at protein concentration about 130 femtomoles (fM). A very good specificity was observed: the measured S protein binding activity to NP mAb was below the limit of detection (LOD). The same was noticed for N protein binding to SP mAb.

Conclusions: The presented SPR assay possesses high sensitivity and selectivity and provides quantitative analysis. This makes it applicable for following the evolution of acute SARS-CoV-2 infection, especially at the early stages of viral replication which can be clinically useful.

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References

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Published

2023-08-14

Issue

Vol. 50 No. 3 (2022)

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Articles

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Copyright (c) 2023 Petia Genova-Kalou, G. Dyankov, H. Kisov, V. Mankov, Evdokiya Hikova, Stefka Krumova, N. Malinowski (Author)

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How to Cite

(1)
Genova-Kalou, P.; Dyankov, G.; Kisov, H.; Mankov, V.; Hikova, E.; Krumova, S.; Malinowski, N. EVALUATION OF INTERACTIONS OF SARS-COV-2 STRUCTURAL PROTEINS WITH SPECIFIC ANTIBODIES BY SPR ASSAY. Probl Infect Parasit Dis 2023, 50 (3), 29-35. https://doi.org/10.58395/peg69k16.

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