Title Investigation and comparison of specific antibodies' affinity interaction with SARS-CoV-2 wild-type, B.1.1.7, and B.1.351 spike protein by total internal reflection ellipsometry /
Authors Plikusienė, Ieva ; Mačiulis, Vincentas ; Juciutė, Silvija ; Maciulevičienė, Rūta ; Balevičius, Saulius ; Ramanavičius, Arūnas ; Ramanavičienė, Almira
DOI 10.3390/bios12050351
Full Text Download
Is Part of Biosensors.. Basel : MDPI. 2022, vol. 12, iss. 5, art. no. 351, p. 1-12.. ISSN 2079-6374
Keywords [eng] total internal reflection ellipsometry ; SARS-CoV-2 ; immune complex ; antibody-antigen interaction
Abstract [eng] SARS-CoV-2 vaccines provide strong protection against COVID-19. However, the emergence of SARS-CoV-2 variants has raised concerns about the efficacy of vaccines. In this study, we investigated the interactions of specific polyclonal human antibodies (pAb-SCoV2-S) produced after vaccination with the Vaxzevria vaccine with the spike proteins of three SARS-CoV-2 variants of concern: wild-type, B.1.1.7, and B.1.351. Highly sensitive, label-free, and real-time monitoring of these interactions was accomplished using the total internal reflection ellipsometry method. Thermodynamic parameters such as association and dissociation rate constants, the stable immune complex formation rate constant (kr), the equilibrium association and dissociation (KD) constants and steric factors (Ps) were calculated using a two-step irreversible binding mathematical model. The results obtained show that the KD values for the specific antibody interactions with all three types of spike protein are in the same nanomolar range. The KD values for B.1.1.7 and B.1.351 suggest that the antibody produced after vaccination can successfully protect the population from the alpha (B.1.1.7) and beta (B.1.351) SARS-CoV-2 mutations. The steric factors (Ps) obtained for all three types of spike proteins showed a 100-fold lower requirement for the formation of an immune complex when compared with nucleocapsid protein.
Published Basel : MDPI
Type Journal article
Language English
Publication date 2022
CC license CC license description