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A Bacterially Expressed SARS-CoV-2 Receptor Binding Domain Fused With Cross-Reacting Material 197 A-Domain Elicits High Level of Neutralizing Antibodies in Mice.
Liu, Liqin; Chen, Tingting; Zhou, Lizhi; Sun, Jie; Li, Yuqian; Nie, Meifeng; Xiong, Hualong; Zhu, Yuhe; Xue, Wenhui; Wu, Yangtao; Li, Tingting; Zhang, Tianying; Kong, Zhibo; Yu, Hai; Zhang, Jun; Gu, Ying; Zheng, Qingbing; Zhao, Qinjian; Xia, Ningshao; Li, Shaowei.
  • Liu L; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Chen T; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Zhou L; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Sun J; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Li Y; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Nie M; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Xiong H; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Zhu Y; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Xue W; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Wu Y; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Li T; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Zhang T; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Kong Z; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Yu H; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Zhang J; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Gu Y; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Zheng Q; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Zhao Q; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
  • Xia N; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, China.
  • Li S; National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
Front Microbiol ; 13: 854630, 2022.
Article in English | MEDLINE | ID: covidwho-1952414
ABSTRACT
The Coronavirus disease 2019 (COVID-19) pandemic presents an unprecedented public health crisis worldwide. Although several vaccines are available, the global supply of vaccines, particularly within developing countries, is inadequate, and this necessitates a need for the development of less expensive, accessible vaccine options. To this end, here, we used the Escherichia coli expression system to produce a recombinant fusion protein comprising the receptor binding domain (RBD) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2; residues 319-541) and the fragment A domain of Cross-Reacting Material 197 (CRM197); hereafter, CRMA-RBD. We show that this CRMA-RBD fusion protein has excellent physicochemical properties and strong reactivity with COVID-19 convalescent sera and representative neutralizing antibodies (nAbs). Furthermore, compared with the use of a traditional aluminum adjuvant, we find that combining the CRMA-RBD protein with a nitrogen bisphosphonate-modified zinc-aluminum hybrid adjuvant (FH-002C-Ac) leads to stronger humoral immune responses in mice, with 4-log neutralizing antibody titers. Overall, our study highlights the value of this E. coli-expressed fusion protein as an alternative vaccine candidate strategy against COVID-19.
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Full text: Available Collection: International databases Database: MEDLINE Type of study: Randomized controlled trials Topics: Vaccines Language: English Journal: Front Microbiol Year: 2022 Document Type: Article Affiliation country: Fmicb.2022.854630

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Full text: Available Collection: International databases Database: MEDLINE Type of study: Randomized controlled trials Topics: Vaccines Language: English Journal: Front Microbiol Year: 2022 Document Type: Article Affiliation country: Fmicb.2022.854630