Cross-reactivity of specific antibodies directed to heat shock proteins from periodontopathogenic bacteria of human origin

This study describes the immunological characterization of two different classes of heat shock proteins isolated from periodontopathogenic bacteria. Analysis of the N-terminal amino acid sequence of a 74-kDa protein from Bacteroides forsythus showed a high degree of homology with the DnaK protein from Escherichia coli. However, this heat shock protein from B. forsythus reacted very weakly with a commercial anti-DnaK polyclonal antibody by dot-blotting. GroEL-like proteins isolated from Actinobacillus actinomycetemcomitans, Porphyromonas gingivalis and B. forsythus showed a high degree of homology of their N-terminal amino acid sequences. In general, polyclonal antibodies raised against each GroEL-like protein showed a high level of cross-reactivity. The cross-reactivity of antibodies to bacterial DnaK-like proteins was much more limited. Our findings suggest that DnaK- and GroEL-like proteins from periodontal pathogens are well conserved and that the GroEL-like proteins resemble each other more closely.