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Disulfide bond reduction corresponds to dimerization and hydrophobicity changes of Clostridium botulinum type A neurotoxin

  
@article{APS3951,
	author = {Jiunn-jye Wey and Shiao-shek Tang and Tzong-yuan Wu},
	title = {Disulfide bond reduction corresponds to dimerization and hydrophobicity changes of Clostridium botulinum type A neurotoxin},
	journal = {Acta Pharmacologica Sinica},
	volume = {27},
	number = {9},
	year = {2016},
	keywords = {},
	abstract = {Aim: To determine the structure factors that mediate the intoxication process of botulinum neurotoxin type A (BoNT/A).
Methods: Triton X-114 phase separation experiments and 1-anilino-8-naphthalene sulfonate binding assay were used to study the structural factor that corresponds to the hydrophobicity change of BoNT/A. In addition, sucrose density gradient centrifugation and a chemical crosslinking study were employed to determine the quaternary structure of BoNT/ A.
Results: Our results demonstrated that in other than acidic conditions, the disulfide reduction is the structural factor that corresponds to the hydrophobicity change of BoNT/A. The quaternary structure of BoNT/A exists as a dimmer in acidic solution (pH 4.5), although the monomeric structure of BoNT/A was reported based on X-ray crystallography.
Conclusion: Disulfide bond reduction is critical for BoNT/A's channel formation and ability to cross endosome membranes. This result implies that compounds that block this disulfide bond reduction may serve as potential therapeutic agents for botulism.},
	issn = {1745-7254},	url = {http://www.chinaphar.com/article/view/3951}
}