scholarly journals Is smaller better? Vaccine targeting recombinant receptor-binding domain might hold the key for mass production of effective prophylactics to fight the COVID-19 pandemic

2020 ◽  
Vol 5 (1) ◽  
Author(s):  
Manish Muhuri ◽  
Guangping Gao
Keyword(s):  
Receptor Binding ◽  
Mass Production ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Recombinant Receptor

scholarly journals Comparative Immunogenicity of the Recombinant Receptor-Binding Domain of Protein S SARS-CoV-2 Obtained in Prokaryotic and Mammalian Expression Systems

Vaccines ◽  
2022 ◽  
Vol 10 (1) ◽  
pp. 96
Author(s):  
Iuliia A. Merkuleva ◽  
Dmitry N. Shcherbakov ◽  
Mariya B. Borgoyakova ◽  
Daniil V. Shanshin ◽  
Andrey P. Rudometov ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Neutralizing Antibodies ◽  
Expression System ◽  
Protein S ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Expression Systems ◽  
Mice Model ◽  
Mammalian Expression ◽  
Recombinant Receptor

The receptor-binding domain (RBD) of the protein S SARS-CoV-2 is considered to be one of the appealing targets for developing a vaccine against COVID-19. The choice of an expression system is essential when developing subunit vaccines, as it ensures the effective synthesis of the correctly folded target protein, and maintains its antigenic and immunogenic properties. Here, we describe the production of a recombinant RBD protein using prokaryotic (pRBD) and mammalian (mRBD) expression systems, and compare the immunogenicity of prokaryotic and mammalian-expressed RBD using a BALB/c mice model. An analysis of the sera from mice immunized with both variants of the protein revealed that the mRBD expressed in CHO cells provides a significantly stronger humoral immune response compared with the RBD expressed in E.coli cells. A specific antibody titer of sera from mice immunized with mRBD was ten-fold higher than the sera from the mice that received pRBD in ELISA, and about 100-fold higher in a neutralization test. The data obtained suggests that mRBD is capable of inducing neutralizing antibodies against SARS-CoV-2.

scholarly journals Yeast-expressed SARS-CoV recombinant receptor-binding domain (RBD219-N1) formulated with aluminum hydroxide induces protective immunity and reduces immune enhancement

Vaccine ◽  
2020 ◽  
Vol 38 (47) ◽  
pp. 7533-7541 ◽  
Author(s):  
Wen-Hsiang Chen ◽  
Xinrong Tao ◽  
Anurodh Shankar Agrawal ◽  
Abdullah Algaissi ◽  
Bi-Hung Peng ◽  
...  
Keyword(s):  
Aluminum Hydroxide ◽  
Receptor Binding ◽  
Protective Immunity ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Recombinant Receptor ◽  
Immune Enhancement

scholarly journals Optimization of the Production Process and Characterization of the Yeast-Expressed SARS-CoV Recombinant Receptor-Binding Domain (RBD219-N1), a SARS Vaccine Candidate

2017 ◽  
Vol 106 (8) ◽  
pp. 1961-1970 ◽  
Author(s):  
Wen-Hsiang Chen ◽  
Shivali M. Chag ◽  
Mohan V. Poongavanam ◽  
Amadeo B. Biter ◽  
Ebe A. Ewere ◽  
...  
Keyword(s):  
Production Process ◽  
Receptor Binding ◽  
Vaccine Candidate ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Recombinant Receptor

Novel and cost-effective refolding of a recombinant receptor binding domain of Plasmodium falciparum EBA-175

2015 ◽  
Vol 50 (12) ◽  
pp. 2177-2181 ◽  
Author(s):  
Bijender Singh ◽  
Puneet Kumar Gupta ◽  
V.S. Chauhan ◽  
C.E. Chitnis
Keyword(s):  
Plasmodium Falciparum ◽  
Receptor Binding ◽  
Cost Effective ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Recombinant Receptor

scholarly journals Cloning, Expression and Biophysical Characterization of a Yeast-expressed Recombinant SARS-CoV-2 Receptor Binding Domain COVID-19 Vaccine Candidate

2020 ◽  
Author(s):  
Wen-Hsiang Chen ◽  
Junfei Wei ◽  
Rakhi Tyagi Kundu ◽  
Rakesh Adhikari ◽  
Zhuyun Liu ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Structural Changes ◽  
Tertiary Structure ◽  
Vaccine Development ◽  
Glycosylation Site ◽  
Binding Domain ◽  
Effective Vaccine ◽  
Receptor Binding Domain ◽  
Biophysical Characterization ◽  
Recombinant Receptor

ABSTRACTCoronavirus disease 2019 (COVID-19) caused by SARS-CoV-2 has now spread worldwide to infect approximately 50 million people, with over 1 million reported deaths, and a safe and effective vaccine remains urgently needed. Based on previous experience developing vaccines against SARS and MERS, we constructed three variants of the recombinant receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein (residues 331-549) in yeast as follows: (1) a “wild type” RBD (RBD219-WT), (2) a deglycosylated form (RBD219-N1) by deleting the first N-glycosylation site, and (3) a combined deglycosylated and cysteine (C538A-mutated variant (RBD219-N1C1)). We compared the expression yields, biophysical characteristics, and functionality of the proteins produced from these constructs. Collectively, these three recombinant protein RBDs showed similar secondary and tertiary structure thermal stability and had the same affinity for their receptor, angiotensin-converting enzyme 2 (ACE-2), suggesting that the selected deletion or mutations did not cause any significant structural changes or alteration of function. However, RBD219-N1C1 had a higher fermentation yield, was easier to purify, and had a lower tendency to form oligomers when compared to the other two proteins and was therefore selected for further vaccine development and evaluation.

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