Antisera Produced Using an E. coli-Expressed SARS-CoV-2 RBD and Complemented with a Minimal Dose of Mammalian-Cell-Expressed S1 Subunit of the Spike Protein Exhibits Improved Neutralization

Yoshizue, Takahiro; Brindha, Subbaian; Wongnak, Rawiwan; Takemae, Hitoshi; Oba, Mami; Mizutani, Tetsuya; Kuroda, Yutaka

doi:10.3390/ijms241310583

Cited by 3 publications

(2 citation statements)

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“…Protein expression and purification were described in detail in our previous report [ 25 , 47 ]. In short, a DNA sequence encoding SARS-CoV2 RBD Omicron BA.5 with a His-tag was inserted into the pET15b vector.…”

Section: Methodsmentioning

confidence: 99%

Non-Glycosylated SARS-CoV-2 Omicron BA.5 Receptor Binding Domain (RBD) with a Native-like Conformation Induces a Robust Immune Response with Potent Neutralization in a Mouse Model

Wongnak,

Brindha,

Oba

et al. 2024

Molecules

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The Omicron BA.5 variant of SARS-CoV-2 is known for its high transmissibility and its capacity to evade immunity provided by vaccine protection against the (original) Wuhan strain. In our prior research, we successfully produced the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein in an E. coli expression system. Extensive biophysical characterization indicated that, even without glycosylation, the RBD maintained native-like conformational and biophysical properties. The current study explores the immunogenicity and neutralization capacity of the E. coli-expressed Omicron BA.5 RBD using a mouse model. Administration of three doses of the RBD without any adjuvant elicited high titer antisera of up to 7.3 × 105 and up to 1.6 × 106 after a booster shot. Immunization with RBD notably enhanced the population of CD44+CD62L+ T cells, indicating the generation of T cell memory. The in vitro assays demonstrated the antisera’s protective efficacy through significant inhibition of the interaction between SARS-CoV-2 and its human receptor, ACE2, and through potent neutralization of a pseudovirus. These findings underscore the potential of our E. coli-expressed RBD as a viable vaccine candidate against the Omicron variant of SARS-CoV-2.

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Section: Methodsmentioning

confidence: 99%

Non-Glycosylated SARS-CoV-2 Omicron BA.5 Receptor Binding Domain (RBD) with a Native-like Conformation Induces a Robust Immune Response with Potent Neutralization in a Mouse Model

Wongnak,

Brindha,

Oba

et al. 2024

Molecules

Self Cite

View full text Add to dashboard Cite

show abstract

“…The study by Yoshizue et al examined the potential of using Escherichia coli -expressed proteins as antigens for subunit vaccines [ 41 ]. They focused on the E. coli -expressed SARS-CoV-2 receptor-binding domain (RBD) of the spike protein as a model.…”

Section: An Overview Of Published Articlesmentioning

confidence: 99%