Recent trends in next generation immunoinformatics harnessed for universal coronavirus vaccine design

Lim, Chin Peng; Kok, Boon Hui; Lim, Hui Ting; Chuah, Candy; Rahman, Badarulhisam Abdul; Majeed, Abu Bakar Abdul; Wykes, Michelle N.; Leow, Chiuan Herng

doi:10.1080/20477724.2022.2072456

Cited by 5 publications

(1 citation statement)

References 195 publications

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“…State-of-the-art approaches to vaccine design include searching for epitopes capable of inducing the most effective humoral and cellular immune response, with methods developed to map and select the most effective epitopes [ 6 , 7 ]. Comparing antibody interactions with different epitopes of different target proteins is important for selecting the most effective vaccine from candidate vaccines and understanding the fundamental basis of the immune response resulting from vaccination [ 8 , 9 , 10 , 11 ]. This study examined the interaction between peptides corresponding to SARS-CoV-2 S-protein sequences and antibodies formed after COVID-19 and anti-COVID-19 vaccination.…”

Section: Introductionmentioning

confidence: 99%

Natural Antibodies Produced in Vaccinated Patients and COVID-19 Convalescents Recognize and Hydrolyze Oligopeptides Corresponding to the S-Protein of SARS-CoV-2

Timofeeva,

Sedykh,

Sedykh

et al. 2023

Vaccines

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The S-protein is the major antigen of the SARS-CoV-2 virus, against which protective antibodies are generated. The S-protein gene was used in adenoviral vectors and mRNA vaccines against COVID-19. While the primary function of antibodies is to bind to antigens, catalytic antibodies can hydrolyze various substrates, including nucleic acids, proteins, oligopeptides, polysaccharides, and some other molecules. In this study, antibody fractions with affinity for RBD and S-protein (RBD-IgG and S-IgG) were isolated from the blood of COVID-19 patients vaccinated with Sputnik V. The fractions were analyzed for their potential to hydrolyze 18-mer oligopeptides corresponding to linear fragments of the SARS-CoV-2 S-protein. Here, we show that the IgG antibodies hydrolyze six out of nine oligopeptides efficiently, with the antibodies of COVID-19-exposed donors demonstrating the most significant activity. The IgGs of control donors not exposed to SARS-CoV-2 were found to be inactive in oligopeptide hydrolysis. The antibodies of convalescents and vaccinated patients were found to hydrolyze oligopeptides in a wide pH range, with the optimal pH range between 6.5 and 7.5. The hydrolysis of most oligopeptides by RBD-IgG antibodies is inhibited by thiol protease inhibitors, whereas S-IgG active centers generally combine several types of proteolytic activities. Ca2+ ions increase the catalytic activity of IgG preparations containing metalloprotease-like active centers. Thus, the proteolytic activity of natural antibodies against the SARS-CoV-2 protein is believed to be due to the similarity of catalytic antibodies’ active centers to canonical proteases. This work raises the question of the possible physiological role of proteolytic natural RBD-IgG and S-IgG resulting from vaccination and exposure to COVID-19.

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