Delineating the susceptibility of botulinum neurotoxins to denaturation through thermal effects

FEBS Letters

Volumn 582, Issue 10, 2008, Pages 1526-1531

  Zhou, Bin ^a   Pellett, Sabine ^b   Tepp, William H ^b   Zhou, Heyue ^a   Johnson, Eric A ^b   Janda, Kim D ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF WISCONSIN   (United States)

Author keywords

Antibody toxin interaction; Botulinum neurotoxin; Surface plasmon resonance; Toxin stability

Indexed keywords

BOTULINUM TOXIN; BOTULINUM TOXIN E; POLYSTYRENE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIBODY SPECIFICITY; ARTICLE; BOTULISM; CLOSTRIDIUM BOTULINUM; CONTROLLED STUDY; DENATURATION; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; MALE; MOUSE; NONHUMAN; PASSIVE IMMUNIZATION; PRIORITY JOURNAL; RAT; SURFACE PLASMON RESONANCE; TEMPERATURE SENSITIVITY;

ANIMALS; ANTIBODIES, MONOCLONAL; BIOLOGICAL ASSAY; BOTULINUM TOXINS; ENZYME-LINKED IMMUNOSORBENT ASSAY; HEAT; HUMANS; MICE; POLYSTYRENES; PROTEIN CONFORMATION; PROTEIN DENATURATION; RABBITS; RATS; SURFACE PLASMON RESONANCE;

ANIMALIA; RATTUS;

EID: 42049104366     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.03.047     Document Type: Article

References (31)

1. Sakaguchi G. Clostridium botulinum toxins. Pharmacol. Ther. 19 (1982) 165-194
2. Hambleton P. Clostridium botulinum toxins: a general review of involvement in disease, structure, mode of action and preparation for clinical use. J. Neurol. 239 (1992) 16-20
3. Johnson E.A., and Bradshaw M. Clostridium botulinum and its neurotoxins: a metabolic and cellular perspective. Toxicon 39 (2001) 1703-1722
4. Gill D.M. Bacterial toxins: a table of lethal amounts. Microbiol. Rev. 46 (1982) 86-94
5. Madsen J.M. Toxins as weapons of mass destruction. A comparison and contrast with biological-warfare and chemical-warfare agents. Clin. Lab. Med. 21 (2001) 593-605
6. Arnon S.S., et al. Botulinum toxin as a biological weapon: medical and public health management. JAMA 285 (2001) 1059-1070
7. Fiock M.A., Devine L.F., Gearinger N.F., Duff J.T., Wright G.G., and Kadull P.J. Studies on immunity to toxins of Clostridium botulinum. VIII. Immunological response of man to purified bivalent AB botulinum toxoid. J. Immunol. 88 (1962) 277-283
8. Hatheway C.L. Toxoid of Clostridium botulinum type F: purification and immunogenicity studies. Appl. Environ. Microbiol. 31 (1976) 234-242
9. Ravichandran E., Al-Saleem F.H., Ancharski D.M., Elias M.D., Singh A.K., Shamim M., Gong Y., and Simpson L.L. Trivalent vaccine against botulinum toxin serotypes A, B, and E that can be administered by the mucosal route. Infect. Immun. 75 (2007) 3043-3054
10. Pier C.L., Tepp W.H., Bradshaw M., Johnson E.A., Barbieri J.T., and Baldwin M.R. Recombinant holotoxoid vaccine against botulism. Infect. Immun. 76 (2008) 437-442
11. Baldwin M.R., Tepp W.H., Przedpelski A., Pier C.L., Bradshaw M., Johnson E.A., and Barbieri J.T. A subunit vaccine against the seven serotypes of botulism. Infect. Immun. (2007)
12. Byrne M.P., and Smith L.A. Development of vaccines for prevention of botulism. Biochimie 82 (2000) 955-966
13. Clayton J., and Middlebrook J.L. Vaccination of mice with DNA encoding a large fragment of botulinum neurotoxin serotype A. Vaccine 18 (2000) 1855-1862
14. Casadevall A. Passive antibody administration (immediate immunity) as a specific defense against biological weapons. Emerg. Infect. Dis. 8 (2002) 833-841
15. Marks J.D. Deciphering antibody properties that lead to potent botulinum neurotoxin neutralization. Mov. Disord. 19 Suppl. 8 (2004) S101-S108
16. Baldwin M.R., Tepp W.H., Przedpelski A., Pier C.L., Bradshaw M., Johnson E.A., and Barbieri J.T. Subunit vaccine against the seven serotypes of botulism. Infect. Immun. 76 (2008) 1314-1318
17. Takeda M., Kasai H., Torii Y., Mukamoto M., Kohda T., Tsukamoto K., and Kozaki S. Protective effect of botulinum C/D mosaic toxoid against avian botulism. J. Vet. Med. Sci. 68 (2006) 325-330
18. Malizio C.J., Goodnough M.C., and Johnson E.A. Purification of Clostridium botulinum type A neurotoxin. Meth. Mol. Biol. 145 (2000) 27-39
19. Prabakaran S., Tepp W., and DasGupta B.R. Botulinum neurotoxin types B and E: purification, limited proteolysis by endoproteinase Glu-C and pepsin, and comparison of their identified cleaved sites relative to the three-dimensional structure of type A neurotoxin. Toxicon 39 (2001) 1515-1531
20. Schantz E.J., and Kautter D.A. Standardized assay for Clostridium botulinum toxins. J. Assoc. Off. Anal. Chem. 61 (1978) 96-99
21. Goodnough M.C., Hammer B., Sugiyama H., and Johnson E.A. Colony immunoblot assay of botulinal toxin. Appl. Environ. Microbiol. 59 (1993) 2339-2342
22. Zhou B., Carney C., and Janda K.D. Selection and characterization of human antibodies neutralizing Bacillus anthracis toxin. Bioorg. Med. Chem. 16 (2008) 1903-1913
23. Pellett S., Tepp W.H., Clancy C.M., Borodic G.E., and Johnson E.A. A neuronal cell-based botulinum neurotoxin assay for highly sensitive and specific detection of neutralizing serum antibodies. FEBS Lett. 581 (2007) 4803-4808
24. Miller K.F., Bolt D.J., and Goldsby R.A. A rapid solution-phase screening technique for hybridoma culture supernatants using radiolabeled antigen and a solid-phase immunoadsorbent. J. Immunol. Meth. 59 (1983) 277-280
25. Houen G., and Koch C. A non-denaturing enzyme linked immunosorbent assay with protein preadsorbed onto aluminum hydroxide. J. Immunol. Met. 200 (1997) 99-105
26. Hollander Z., and Katchalski-Katzir E. Use of monoclonal antibodies to detect conformational alterations in lactate dehydrogenase isoenzyme 5 on heat denaturation and on adsorption to polystyrene plates. Mol. Immunol. 23 (1986) 927-933
27. Friguet B., Djavadi-Ohaniance L., and Goldberg M.E. Some monoclonal antibodies raised with a native protein bind preferentially to the denatured antigen. Mol. Immunol. 21 (1984) 673-677
28. Kukreja R.V., and Singh B.R. Comparative role of neurotoxin-associated proteins in the structural stability and endopeptidase activity of botulinum neurotoxin complex types A and E. Biochemistry (2007)
29. Brandau D.T., Joshi S.B., Smalter A.M., Kim S., Steadman B., and Middaugh C.R. Stability of the Clostridium botulinum type A neurotoxin complex: an empirical phase diagram based approach. Mol. Pharm. 4 (2007) 571-582
30. Fischer A., Garcia-Rodriguez C., Geren I., Lou J., Marks J.D., Nakagawa T., and Montal M. Molecular architecture of botulinum neurotoxin e revealed by single particle electron microscopy. J. Biol. Chem. 283 (2008) 3997-4003
31. Razai A., et al. Molecular evolution of antibody affinity for sensitive detection of botulinum neurotoxin type A. J. Mol. Biol. 351 (2005) 158-169