Abstract
The response of Clostridium botulinum type A strain to elevated temperature was investigated with respect to its growth pattern, and qualitative and quantitative alterations in the protein profile. Transfer of the mid log phase cells from 37°C to 45°C repressed the synthesis of several cellular proteins and concomitantly, synthesis of some proteins including a 33 kDa polypeptide, was markedly enhanced. The induction and synthesis of 33 kDa protein was also observed in 2-D gel analysis of the cells grown at 37°C and 45°C. Immunoblot analysis revealed that 33 kDa protein is a hemagglutinin component of the neurotoxin complex of type A Clostridium botulinum. From these findings we conclude that the 33 kDa protein component of type A neurotoxin complex, known to protect and stabilise neurotoxins from a hostile environment, is a Heat Shock Protein (HSP).
Original language | English (US) |
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Pages (from-to) | 309-317 |
Number of pages | 9 |
Journal | Botulinum Journal |
Volume | 1 |
Issue number | 3 |
DOIs | |
State | Published - 2009 |
Keywords
- Chaperone
- HSPs
- Heat shock proteins
- Heat stress
- Hemagglutinin
- Immunoblot
- Neurotoxin
- Neurotoxin complex
- Protection
ASJC Scopus subject areas
- Biochemistry
- Pharmacology, Toxicology and Pharmaceutics(all)
- Cellular and Molecular Neuroscience