Cloning, high level expression and immunogenicity of 1163-1256 residues of C-terminal heavy chain of C. botulinum neurotoxin type E

Biologicals

Volumn 38, Issue 2, 2010, Pages 260-264

  Mansour, Abdoulreza Agheli ^a   Mousavi, Seyed Latif ^b   Rasooli, Iraj ^b   Nazarian, Shahram ^c   Amani, Jafar ^a   Farhadi, Nima ^a  

^a BAQIYATALLAH UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^b SHAHED UNIVERSITY   (Iran)

^c IMAM HOSSEIN UNIVERSITY   (Iran)

Author keywords

Binding domain; Botulinum neurotoxin; Immunogenicity; Synthetic gene

Indexed keywords

AMINO ACID; CARBOXY TERMINAL BOTULINUM TOXIN E HEAVY CHAIN; GANGLIOSIDE; RECOMBINANT PROTEIN; SYNAPTOTAGMIN; UNCLASSIFIED DRUG;

AMINO ACID SYNTHESIS; ANIMAL EXPERIMENT; ARTICLE; BACTERIAL STRAIN; CODON USAGE; CONTROLLED STUDY; DRUG BINDING; DRUG SCREENING; ESCHERICHIA COLI; EXPRESSION VECTOR; GEL CHROMATOGRAPHY; GENE EXPRESSION; HEAVY CHAIN; IMMUNIZATION; IMMUNOGENICITY; MALE; MOLECULAR CLONING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTECTION; PROTEIN CONFORMATION; PROTEIN PURIFICATION; RECOMBINANT PLASMID;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODY FORMATION; BACTERIAL VACCINES; BASE SEQUENCE; BOTULINUM TOXINS; BOTULISM; CLONING, MOLECULAR; CLOSTRIDIUM BOTULINUM TYPE E; GENE EXPRESSION; MALE; MICE; MICE, INBRED BALB C; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; TRANSFORMATION, BACTERIAL; VACCINES, SYNTHETIC;

ESCHERICHIA COLI; MUS;

EID: 77950691735     PISSN: 10451056     EISSN: 10958320     Source Type: Journal    
DOI: 10.1016/j.biologicals.2009.09.008     Document Type: Article

References (31)

1. Li L., Singh B.R. Structure-function relationship of clostridial neurotoxins. J Toxicol Toxin Rev 1999, 18:95-112.
2. Singh B.R. Intimate details of the most poisonous poison. Nat Struct Biol 2000, 7:617-619.
3. Yu Y.Z., Sun Z.W., Wang S., Yu W.Y. High-level expression of the Hc domain of Clostridium botulinum neurotoxin serotype A in Escherichia coli and its immunogenicity as an antigen. Chin J Biotechnol 2007, 3:812-817.
4. Arnon S.S., Schechter R., Inglesby T.V., Henderson D.A., Bartlett J.G., Ascher M.S., et al. Botulinum toxin as a biological weapon: medical and public health management. J Am Med Assoc 2001, 285:1059-1070.
5. Fiock M.A., Cardella M.A., Gearinger N.F. Studies on immunity to toxins of Clostridium botulinum. Ix. Immunologic response of man to purified pentavalent abcde botulinum toxiod. J Immunol 1963, 90:697-702.
6. Wright G.G., Duff J.T., Flock M.A., Devlin H.B., Soderstrom R.L. Studies on immunity to toxins of Clostridium botulinum. V. Detoxification of purified type A and type B toxins, and the antigenicity of univalent and bivalent aluminium phosphate adsorbed toxoids. J Immunol 1960, 84:384-389.
7. Boles J., West M., Montgomery V., Tammariello R., Pitt M.L., Gibbs P., et al. Recombinant C fragment of botulinum neurotoxin B serotype (rBoNTB (HC)) immune response and protection in the rhesus monkey. Toxicon 2006, 47:877-884.
8. Clayton M.A., Clayton J.M., Brown D.R., Middlebrook J.L. Protective vaccination with a recombinant fragment of Clostridium botulinum neurotoxin serotype A expressed from a synthetic gene in Escherichia coli. Infect Immun 1995, 63:2738-2742.
9. Dertzbaugh M.T., West M.W. Mapping of protective and cross-reactive domains of the type A neurotoxin of Clostridium botulinum. Vaccine 1996, 14:1538-1544.
10. LaPenotiere H.F., Clayton M.A., Middlebrook J.L. Expression of a large, nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen. Toxicon 1995, 33:1383-1386.
11. Lee J.C., Hwang H.J., Sakaguchi Y., Yamamoto Y., Arimitsu H., Tsuji T., et al. C terminal half fragment (50kDa) of heavy chain components of Clostridium botulinum type C and D neurotoxins can be used as an effective vaccine. Microbiol Immunol 2007, 51:445-455.
12. Webb R.P., Smith T.J., Wright P.M., Montgomery V.A., Meagher M.M., Smith L.A. Protection with recombinant Clostridium botulinum C1 and D binding domain subunit (Hc) vaccines against C and D neurotoxins. Vaccine 2007, 25:4273-4282.
13. Baldwin M.R., Tepp W.H., Pier C.L., Bradshaw M., Ho M., Wilson B.A., et al. Characterization of the antibody response to the receptor binding domain of botulinum neurotoxin serotypes A and E. Infect Immun 2005, 73:6998-7005.
14. Atassi M.Z., Dolimbek B.Z., Hayakari M., Middlebrook J.L., Whitney B., Oshima M. Mapping of the antibody-binding regions on botulinum neurotoxin H-chain domain 855-1296 with antitoxin antibodies from three host species. J Protein Chem 1996, 15:691-700.
15. Atassi M.Z., Oshima M. Structure, activity, and immune (T and B cell) recognition of botulinum neurotoxins. Crit Rev Immunol 1999, 19:219-260.
16. Byrne M.P., Smith L.A. Development of vaccines for prevention of botulism. Biochimie 2000, 82:955-966.
17. Oshima M., Hayakari M., Middlebrook J.L., Atassi M.Z. Immune recognition of botulinum neurotoxin type A: regions recognized by T cells and antibodies against the protective H(C) fragment (residues 855-1296) of the toxin. Mol Immunol 1997, 34:1031-1040.
18. Oshima M., Middlebrook J.L., Atassi M.Z. Antibodies and T cells against synthetic peptides of the C-terminal domain (Hc) of botulinum neurotoxin type A and their cross-reaction with Hc. Immunol Lett 1998, 60:7-12.
19. Rummel A., Bade S., Alves J., Bigalke H., Binz T. Two carbohydrate binding sites in the H (CC)-domain of tetanus neurotoxin are required for toxicity. J Mol Biol 2003, 326:835-847.
20. Kitamura M., Takamiya K., Aizawa S., Furukawa K., Furukawa K. Gangliosides are the binding substances in neural cells for tetanus and botulinum toxins in mice. Biochim Biophys Acta 1999, 1441:1-3.
21. Kozaki S., Kamata Y., Watarai S., Nishiki T., Mochida S. Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins. Microb Pathog 1998, 25:91-99.
22. Li L., 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 1998, 7:215-226.
23. Ginalski K., Venclovas C., Lesyng B., Fidelis K. Structure-based sequence alignment for the beta-trefoil subdomain of the clostridial neurotoxin family provides residue level information about the putative ganglioside binding site. FEBS Lett 2000, 482:119-124.
24. Montecucco C., Rossetto O., Schiavo G. Presynaptic receptor arrays for clostridial neurotoxins. Trends Microbiol 2004, 12:442-446.
25. Simpson L.L. Identification of the characteristics that underlie botulinum toxin potency: implications for designing novel drugs. Biochimie 2000, 82:943-953.
26. Tavallaie M., Chenal A., Gillet D., Pereira Y., Manich M., Gibert M., 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 2004, 572:299-306.
27. Zhou Y., 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 2004, 34:8-16.
28. Kubota T., Watanabe T., Yokosawa N., Tsuzuki K., Indoh T., Moriishi K., et al. Epitope regions in the heavy chain of Clostridium botulinum type E neurotoxin recognized by monoclonal antibodies. Appl Environ Microbiol 1997, 63:1214-1218.
29. Romanos M.A., Makoff A.J., Fairweather N.F., Beesley K.M., Slater D.E., Rayment F.B., et al. Expression of tetanus toxin fragment C in yeast: gene synthesis is required to eliminate fortuitous polyadenylation sites in AT-rich DNA. Nucleic Acids Res 1991, 19:1461-1467.
30. Makoff A.J., Oxer M.D., Romanos M.A., Fairweather N.F., Ballantine S. Expression of tetanus toxin fragment C in E. coli: high level expression by removing rare codons. Nucleic Acids Res 1989, 17:10191-10202.
31. Yu Y.Z., Li N., Wang R.L., Zhu H.Q., Wang S., Yu W.Y., et al. Evaluation of a recombinant Hc of Clostridium botulinum neurotoxin serotype F as an effective subunit vaccine. Clin Vaccine Immunol 2008, 15:1819-1823.