Predictions of secondary structure and solvent accessibility of the light chain of the clostridial neurotoxins

Journal of Natural Toxins

Volumn 7, Issue 3, 1998, Pages 227-238

  Lebeda, Frank J ^a   Olson, Mark A ^a  

^a UNITED STATES ARMY MEDICAL RESEARCH INSTITUTE OF INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN; EPITOPE; METALLOPROTEINASE; SOLVENT; TETANOSPASMIN; TETANUS TOXIN; THERMOLYSIN; ZINC;

ALGORITHM; ARTIFICIAL NEURAL NETWORK; BINDING SITE; CHEMISTRY; COMPARATIVE STUDY; CONFERENCE PAPER; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY;

ALGORITHMS; BINDING SITES; BOTULINUM TOXINS; EPITOPES; METALLOENDOPEPTIDASES; NEURAL NETWORKS (COMPUTER); PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SOLVENTS; TETANUS TOXIN; THERMOLYSIN; ZINC;

EID: 0032188988     PISSN: 10588108     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper

References (33)

1. Bavari, S., Pless, D., Torres, E. R., Lebeda, F. J., and Olson, M. A., (1998). Identifying the principle protective determinants of botulinum neurotoxins. Vaccine, in press.
2. Bode, W., Gomis-Rüth, F.-Z., and Stöckler, W. (1993). Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Metturn) and topologies and should be grouped into a common family, the 'metzincins.' FEBS Lett. 331, 134-140.
3. Collingridge, G. L., and Herron, C. E. (1985). Effects of tetanus toxin on GABA synapses in the mammalian central nervous system. In: Seventh International Conference on Tetanus, G. Nistico, P. Mastroeni, and M. Pitzurra, pp. 127-142. Gangemi Publ. Co., Rome.
4. Devereux, J., Haeberli, P., and Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nuc. Acids Res. 12, 387-395.
5. Dolly, J. O., de Paiva, A., Poulain, B., Foran, P., Ashton, A., and Tauc, L. (1992). Insights into the neuronal binding, uptake and intracellular activity of botulinum neurotoxins. In: Bacterial Protein Toxins. Zbl. Bakt. Suppl. 23, Witholt et al. (Eds.), pp. 31-45. Gustav Fischer, Stuttgart, Jena, New York.
6. Foran, P., Lawrence, G. W., Shone, C. C., Foster, K. A., and Dolly, J. O. (1996). Botulinum neurotoxin C1 cleaves both syntoxin and SNAP-25 in intact and penneabilized chromaffin cells: Correlation with its blockade of catecholamine release. Biochemistry 35, 2630-2636.
7. Foran, P., Shone, C. C., and Dolly, J. O. (1994). Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments. Biochemistry 33, 15365-15374.
8. Holmes, M. A., and Matthews, B. W. (1982). Structure of thermolysin refined at 1.6 Angstroms resolution. J. Mol. Biol. 160, 623-639.
9. Jongeneel, C. V., Bouvier, J., and Bairoch, A. (1989). A unique signature identifies a family of zinc-dependent matallopeptidases. FEBS Lett. 242, 211-214.
10. Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
11. Lacey, B., Cohen, A., and Steven, R. C. (1997). The three-dimensional X-ray crystal structure of botulinum neurotoxin serotype A. Abstract, "Second International Meeting on the Molecular Genetics and Pathogenesis of the Clostridia," Ohzain, France, p. 37.
12. Lebeda, F. J., and Olson, M. A. (1994). Secondary structural predictions for the clostridial neurotoxins. Proteins: Struct. Funct. Gen. 20, 293-300.
13. Lebeda, F. J., and Olson, M. A. (1997). Predicting differential antigen-antibody contact regions based on solvent accessibility. J. Prot. Chem. 16, 607-618.
14. Lebeda, F. J., and Singh, B. R. (1998). Membrane channel activity and translocation of tetanus and botulinum neurotoxins. J. Natural Tox., in press.
15. Lebeda, F. J., Umland, T. C., Sax, M., and Olson, M. A. (1998). Accuracy of secondary structure and solvent accessibility predictions for a clostridial neurotoxin C-fragment. J. Prot. Chem. 17, 311-318.
16. Miyoshi, S.-I., and Shinoda, S. (1997). Bacterial metalloprotease as the toxic factor in infection. J. Toxicol., Toxin Rev. 16, 177-194.
17. Montecucco, C., and Schiavo, G. (1994). Mechanism of action of tetanus and botulinum neurotoxins. Molec. Microbiol. 13, 1-8.
18. Niemann, H., Blasi, J., and Jahn, R. (1994). Clostridial neurotoxins: New tools for dissecting exocytosis. Trends Cell Biol. 4, 179-185.
19. Rost, B. (1996). PHD: Predicting one-dimensional protein structure by profile based neural networks. Meth. Enzymol. 266, 525-539.
20. Rost, B., and Sander, C. (1993a). Redefining the goals of protein secondary structure prediction. J. Mol. Biol. 235, 13-26.
21. Rost, B., and Sander, C. (1993b). Prediction of protein structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
22. Rost, B., and Sander, C. (1994a). Conservation and prediction of solvent accessibility in protein families. Proteins: Struct. Funct. Gen. 20, 216-226.
23. Rost, B., and Sander, C. (1994b). Combining evolutionary information and neural networks to predict protein secondary structure. Proteins: Struct. Funct. Gen. 19, 55-72.
24. Sander, C., and Schneider, R. (1991). Database of homology-derived structures and the structural meaning of sequence alignment. Proteins: Struct. Funct. Gen. 9, 56-68.
25. Schmidt, J. J., and Bostian, K. A. (1995). Proteolysis of synthetic peptides by type A botulinum neurotoxin. J. Prot. Chem. 14, 703-708.
26. Schmidt, J. J., and Bostian, K. A. (1997). Endopeptidase activity of type A botulinum neurotoxin: Substrate requirements and activation by serum albumin. J. Prot. Chem. 16, 19-26.
27. Shone, C. C., Quinn, C. P., Wait, R., Hallis, B., Fooks, S. G., and Hambleton, P. (1993). Proteolytic cleavage of synthetic fragments of vesicle-associated membrane protein, isoform-2, by botulinum type B neurotoxin. Eur. J. Biochem. 217, 965-971.
28. Simpson, L. L. (1993). Current concepts on the mechanism of action of clostridial neurotoxins. In: Botulinum and Tetanus Neurotoxins: Neurotransmission and Biomedical Aspects, D. A. DasGupta (Ed.), pp. 5-15. Plenum Press, New York.
29. Singh, B. R., and DasGupta, B. R. (1989a). Molecular topography and secondary structure comparisons of botulinum neurotoxin types A, B and E. Molec. Cell. Biochem. 86, 87-95.
30. Singh, B. R., and DasGupta, B. R. (1989b). Structure of heavy and light chain subunits of type A botulinum neurotoxin analyzed by circular dichroism and fluorescence measurements. Molec. Cell Biochem. 85, 67-73.
31. Singh, B. R., and DasGupta, B. R. (1989c). Changes in molecular topography of the light and heavy chains of type A botulinum neurotoxin following their separation. Biophys. Chem. 34, 259-267.
32. c of tetanus neurotoxin. Nature Struct. Biol. 4, 788-792.
33. Williamson, L. C., Halpern, J. L., Montecucco, C., Brown, J. E., and Neale, E. A. (1996). Clostridial neurotoxins and substrate proteolysis in intact neurons. Botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa. J. Biol. Chem. 271, 7694-7699.