Open AccessProtection Afforded by Heat Shock Protein 60 fromFrancisella tularensisIs Due to Copurified Lipopolysaccharide
Author(s) -
M. Gill Hartley,
M Green,
Glyn Choules,
Donna P. Rogers,
Dianne Rees,
Sarah L. Newstead,
Anders Sjöstedt,
Richard W. Titball
Publication year - 2004
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.72.7.4109-4113.2004
Subject(s) - francisella tularensis , lipopolysaccharide , biology , heat shock protein , shock (circulatory) , microbiology and biotechnology , tularemia , francisella , virology , immunology , virulence , biochemistry , medicine , gene
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.