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Expression, purification, and characterisation of recombinant ferritin in insect cells using the baculovirus expression system.

Authors
  • Qu, Zhehui1, 2
  • Li, Mingzhu1
  • Guo, Yongli3
  • Liu, Yue1
  • Wang, Junwei4
  • Gao, Mingchun5
  • 1 Department of Preventive Veterinary Medicine, College of Veterinary Medicine, Northeast Agricultural University, 600 Changjiang Road, Xiangfang District, Harbin, 150030, Heilongjiang, People's Republic of China. , (China)
  • 2 College of Animal Science and Veterinary Medicine, Xinyang Agriculture and Forestry University, Xinyang, 464000, Henan, People's Republic of China. , (China)
  • 3 Animal Disease Prevention and Control Center of Heilongjiang Province, Harbin, 150069, Heilongjiang, People's Republic of China. , (China)
  • 4 Department of Preventive Veterinary Medicine, College of Veterinary Medicine, Northeast Agricultural University, 600 Changjiang Road, Xiangfang District, Harbin, 150030, Heilongjiang, People's Republic of China. [email protected] , (China)
  • 5 Department of Preventive Veterinary Medicine, College of Veterinary Medicine, Northeast Agricultural University, 600 Changjiang Road, Xiangfang District, Harbin, 150030, Heilongjiang, People's Republic of China. [email protected] , (China)
Type
Published Article
Journal
Biotechnology Letters
Publisher
Springer-Verlag
Publication Date
Nov 13, 2019
Identifiers
DOI: 10.1007/s10529-019-02755-6
PMID: 31720971
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Ferritin is an attractive vector for the delivery of drug molecules and antigen proteins because of its unique structural and biochemical features. In this study, recombinant ferritin from Helicobacter pylori was expressed in the soluble form employing the baculovirus expression system. The optimum conditions for producing recombinant ferritin comprised MOI 5 of rBV-ferritin for 96 h of infection. The recombinant ferritin was purified by Ni Sepharose™ 6 Fast Flow, with a purity and yield of 92.5% and 11.25 mg/L, respectively. In addition, the recombinant ferritin showed a multimeric structure under non-denaturing conditions, as well as self-assembled spherical cage architecture with a diameter of approximately 12 nm. Dot-ELISA results suggested that the His-tag at the N-terminus likely existed on the surface of the recombinant ferritin. Recombinant ferritin was produced by the baculovirus expression system, which has the potential to display exogenous proteins, and may aid in the delivery of drugs for disease prevention and treatment.

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