Related Experiment Video
Updated: Jun 19, 2026

Visualization of Bacterial Toxin Induced Responses Using Live Cell Fluorescence Microscopy
Published on: October 1, 2012
[Peptide bond scission of staphylococcal enterotoxin C2 and related factors]
Yue-Bin Ying1, Hong-Ying Sun, Ding Ding
1Institute of Pharmacology, Toxicology and Biological Pharmaceutics, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou, 310058, China.
Objective:
To investigate the limited digestion of recombinant staphylococcal enterotoxin C2 (SEC2-His)in different conditions.
Methods:
The purified recombinant SEC2-His was treated with different reagents and the cleavage of rSEC2 molecule was observed by SDS-PAGE.
Result:
The cleavage occurred in positions Cys93-Cys110 of the disulfide loop. Complete auto-cleavage of recombinant SEC2 was observed in solution at 37degrees within 24 hrs, and that was accelerated under alkaline conditions. The auto-cleavage of the recombinant protein was inhibited in the presence of beta-ME (2%), PMSF (5-10 mmol/L), imidazole (1 mol/L) or crude E.coli lysate. Non-specific degradation of recombinant SEC2 was promoted with the increasing of the concentration of H(2)O(2).
Conclusion:
The recombinant SEC2-His is broken down in special site of protein, which may be associated with the protein structure.
Related Concept Videos
Bacterial Toxins
Peptide Bonds
Determinants of Bacterial Pathogenicity and Virulence
Caspases
Fusion of Secretory Vesicles with the Plasma Membrane
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
Diphtheria

