SNU CBE

Functional Expression of the Recombinant Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm of Escherichia coli

2022 · Bioengineering

저자

Woo Sung Kim, Ji Hyun Kim, Jisun Lee, Su Yeon Ka, Hee Do Chae, Inji Jung, 정상택 (Sang Taek Jung), Jung‐Hyun Na

연구주제

SARS-CoV-2 and COVID-19 Research · Viral Infectious Diseases and Gene Expression in Insects · Protein purification and stability

NTIS 과학기술표준분류

가장 가까운 분류(생명과학 > 산업바이오 > 기능성 바이오소재)가 화학·화공 범위 밖이다. 배정 근거: 지원 과제의 분류와 AI 키워드가 잡은 과제의 분류를 반씩.

AI 연구 키워드·방법

disulfide bond formation 대장균 발현 시스템 periplasmic expression 스파이크 수용체결합도메인(RBD)

키워드 (OpenAlex)

Omicron variant spike protein receptor-binding domain recombinant protein expression Escherichia coli periplasm disulfide bond formation protein disulfide isomerase protein folding sotrovimab

초록

A new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant known as Omicron has caused a rapid increase in recent global patients with coronavirus infectious disease 2019 (COVID-19). To overcome the COVID-19 Omicron variant, production of a recombinant spike receptor binding domain (RBD) is vital for developing a subunit vaccine or a neutralizing antibody. Although bacterial expression has many advantages in the production of recombinant proteins, the spike RBD expressed in a bacterial system experiences a folding problem related to disulfide bond formation. In this study, the soluble Omicron RBD was obtained by a disulfide isomerase-assisted periplasmic expression system in Escherichia coli. The Omicron RBD purified from E. coli was very well recognized by anti-SARS-CoV-2 antibodies, sotrovimab (S309), and CR3022, which were previously reported to bind to various SARS-Co…

이 논문을 지원한 국가R&D 과제 (NTIS 성과)

연도과제부처사업수행기관NTIS 분류(1순위)
2022나노바디 기반 동물생리활성물질자원 거점은행과학기술정보통신부국가생명연구자원선진화사업(과기부)상지대학범위 밖
2022융합중개의과학 교육연구단교육부4단계두뇌한국21사업(R&D)고려대학–

인접 그래프

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교수 1

정상택

연구주제 1

SARS-CoV-2 and COVID-19 Research

키워드 2

스파이크 수용체결합도메인(RBD) · 대장균 발현 시스템