Protection afforded by heat shock protein 60 from Francisella tularensis is due to copurified lipopolysaccharide
Related Experiment Video
Updated: Aug 23, 2026

Method for the Isolation of Francisella tularensis Outer Membranes
Published on: June 29, 2010
M G Hartley1, M Green, G Choules
1Bldg. 245, Defence Science and Technology Laboratory, Porton Down, Salisbury, Wilts SP4 0NS, United Kingdom. mghartley@dstl.gov.uk
Abstract:
Heat shock proteins (Hsps) have attracted significant attention as protective antigens against a range of diseases caused by bacterial pathogens. However, more recently there have been suggestions that the protective response is due to the presence of peptide components other than Hsps. We have shown that mice that had been immunized with purified heat shock protein 60 (Hsp60) isolated from Francisella tularensis were protected against a subsequent challenge with some strains of the bacterium. However, this protection appeared to be due to trace amounts of lipopolysaccharide, which were too low to be detected by using the Limulus amoebocyte lysate assay. This finding raises the possibility that the protection afforded by other bacterial Hsp60 proteins may be due to trace quantities of polysaccharide antigens carried by and acting in conjunction with the Hsps.
Related Concept Videos
Other Stress Responses in Bacteria
Bacterial Protein Maturation
Molecular Chaperones and Protein Folding
The...
Formation of Lipopolysaccharides
Diversity of Archaea IV
Regulation of the Unfolded Protein Response

