Improved soluble expression and characterization of the Hc domain of Clostridium botulinum neurotoxin serotype A in Escherichia coli by using a PCR-synthesized gene and a Trx co-expression strain

Protein Expression and Purification

Volumn 71, Issue 1, 2010, Pages 79-84

  Chen, Rongchang ^a,b   Shi, Jing ^a   Cai, Kun ^a   Tu, Wei ^a   Hou, Xiaojun ^a   Liu, Hao ^a   Xiao, Le ^a   Wang, Qin ^a   Tang, Yunming ^b   Wang, Hui ^a  

^a BEIJING INSTITUTE OF MICROBIOLOGY AND EPIDEMIOLOGY   (China)

^b SOUTHWEST UNIVERSITY   (China)

Author keywords

PCR synthesized gene; Receptor binding activity; Trx co expression strain

Indexed keywords

ANTIBODY; BOTULINUM TOXIN A; GANGLIOSIDE; THIOREDOXIN;

ANIMAL; ARTICLE; BAGG ALBINO MOUSE; BIOCHEMISTRY; CHEMISTRY; CLOSTRIDIUM BOTULINUM; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; FEMALE; GENETICS; IMMUNOLOGY; ISOLATION AND PURIFICATION; METABOLISM; METHODOLOGY; MOUSE; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SERUM; SOLUBILITY; TITRIMETRY;

ANIMALS; ANTIBODIES; BIOCHEMISTRY; BOTULINUM TOXIN TYPE A; CLOSTRIDIUM BOTULINUM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; FEMALE; GANGLIOSIDES; MICE; MICE, INBRED BALB C; POLYMERASE CHAIN REACTION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SERUM; SOLUBILITY; THIOREDOXINS; TITRIMETRY;

ANIMALIA; BACTERIA (MICROORGANISMS); CLOSTRIDIUM BOTULINUM; ESCHERICHIA COLI;

EID: 77049123910     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.11.007     Document Type: Article

References (22)

1. Gilsdorf J., Gul N., and Smith L.A. Expression, purification, and characterization of Clostridium botulinum type B light chain. Protein Expr. Purif. 46 (2006) 256-267
2. Schiavo G., Matteoli M., and Montecucco C. Neurotoxins affecting neuroexocytosis. Physiol. Rev. 80 (2000) 717-766
3. Turton K., Chaddock J.A., and Acharya K.R. Botulinum and tetanus neurotoxins: structure, function and therapeutic utility. Trends Biochem. Sci. 27 (2002) 552-558
4. CC-domain of tetanus neurotoxin are required for toxicity. J. Mol. Biol. 326 (2003) 835-847
5. T1b as a complementary receptor component for Clostridium botulinum neurotoxins. Microb. Pathog. 25 (1998) 91-99
6. Smith L.A., and Byrne M.P. Vaccines for preventing botulism. In: Brin M.F., Jankovic J., and Hallett M. (Eds). Scientific and Therapeutic Aspects of Botulinum Toxin (2002), Lippincott Williams and Wilkins, Philadelphia 427-437
7. Simpson L.L. Identification of the characteristics that underlie botulinum toxin potency: implications for designing novel drugs. Biochimie 82 (2000) 943-953
8. Smith L.A. Development of recombinant vaccines for botulinum neurotoxin. Toxicon 36 (1998) 539-548
9. Tavallaie M., Chenal A., Gillet D., et al. Interaction between the two subdomains of the C-terminal part of the botulinum neurotoxin A is essential for the generation of protective antibodies. FEBS Lett. 572 (2004) 299-306
10. LaPenotiere H.F., Clayton M.A., and Middlebrook J.L. Expression of a large nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen. Toxicon 33 (1995) 1383-1386
11. Clayton M.A., Clayton J.M., Brown D.R., et al. Protective vaccination with a recombinant fragment of Clostridium botulinum neurotoxin serotype A expressed from a synthetic gene in Escherichia coli. Infect. Immun. 63 (1995) 2728-2742
12. Woodward L.A., Arimitsu H., Hirst R., et al. Expression of Hc subunits from Clostridium botulinum type C and D and their evaluation as candidate vaccine antigens in mice. Infect. Immun. 71 (2003) 2941-2944
13. Holley J.L., Mike E., Margaret M., et al. Cloning, expression and evaluation sub-unit vaccine against clostridium type F toxin. Vaccine 19 (2001) 288-297
14. Byrne M.P., Smith T.J., Montgomery V.A., et al. Purification, potency, and efficacy of the botulinum neurotoxin type A binding domain from Pichia pastoris as a recombinant vaccine candidate. Infect. Immun. 66 (1998) 4817-4822
15. Potter K.J., Bevins M.A., Vassilieva E.V., et al. Production and purification of the heavy chain fragment C of botulinum neurotoxin serotype B expressed in the methyltrophic yeast Pichia pastoris. Protein Expr. Purif. 13 (1998) 357-365
16. Byrne M.F., Titball R.W., Holley J., et al. Fermentation, purification and efficacy of a recombinant vaccine candidate against botulinum neurotoxin type F from Pichia pastoris. Protein Expr. Purif. 18 (2000) 327-337
17. Zhou Y., and Singh B.R. Cloning, high level expression, single step purification and binding activity of His6-tagged recombinant type B botulinum neurotoxin heavy chain transmembrane and binding domain. Protein Expr. Purif. 34 (2004) 8-16
18. Emsley P., Fotinou C., Black I., et al. The structures of the HC fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding. J. Biol. Chem. 275 (2000) 8889-8894
19. Singh B.R. Intimate details of the most poisonous poison. Nat. Struct. Biol. 7 (2000) 617-619
20. Sharma S., Zhou Y., and Sing B.R. Cloning, expression and purification of C-terminal quarter of heavy chain of botulinum neurotoxin type A. Protein Expr. Purif. 45 (2006) 288-295
21. Li L., and Singh B.R. Isolation of synaptotagmin as a receptor for types A and E botulinum neurotoxin and analysis of their comparative binding using a new microtiter plate assay. J. Nat. Toxins 7 (1998) 215-226
22. Hoover D.M., and Lubkowski J. DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis. Nucleic Acids Res. 30 (2002) e43