Related Experiment Video
Updated: Mar 7, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
Published on: January 3, 2012
Thermal stability and structural changes in bacterial toxins responsible for food poisoning
Paulina Regenthal1, Jesper S Hansen1, Ingemar André2
1Department of Experimental Medical Science, Lund University, BMC, Lund, Sweden.
Abstract:
The staphylococcal enterotoxins (SEs) are secreted by the bacteria Staphylococcus aureus and are the most common causative agent in staphylococcal food poisoning. The staphylococcal enterotoxin A (SEA) has been associated with large staphylococcal food poisoning outbreaks, but newer identified SEs, like staphylococcal enterotoxin H (SEH) has recently been shown to be present at similar levels as SEA in food poisoning outbreaks. Thus, we set out to investigate the thermo-stability of the three-dimensional structures of SEA, SEH and staphylococcal enterotoxin E (SEE), since heat inactivation is a common method to inactivate toxins during food processing. Interestingly, the investigated toxins behaved distinctly different upon heating. SEA and SEE were more stable at slightly acidic pH values, while SEH adopted an extremely stable structure at neutral pH, with almost no effects on secondary structural elements upon heating to 95°C, and with reversible formation of tertiary structure upon subsequent cooling to room temperature. Taken together, the data suggests that the family of staphylococcal enterotoxins have different ability to withstand heat, and thus the exact profile of heat inactivation for all SEs causing food poisoning needs to be considered to improve food safety.
Related Concept Videos
Protein Denaturation
Physical Methods for Controlling Microbial Growth: Temperature
Bacterial Protein Maturation
Factors Influencing Microbial Growth: Temperature
Diversity of Archaea IV
Other Stress Responses in Bacteria

