Cross-reactivity of specific antibodies directed to heat shock proteins from periodontopathogenic bacteria and of human origin [corrected].
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.
Hinode
D
D
Department of Preventive Dentistry, School of Dentistry, University of Tokushima, Tokushima City, Japan.
Nakamura
R
R
Grenier
D
D
Mayrand
D
D
D000595:Amino Acid Sequence; D000907:Antibodies, Bacterial / Q000276:immunology*; D000918:Antibody Specificity / Q000276:immunology*; D001419:Bacteria / Q000235:genetics / Q000276:immunology*; D003429:Cross Reactions / Q000276:immunology; D006360:Heat-Shock Proteins / Q000032:analysis / Q000235:genetics / Q000276:immunology* / Q000302:isolation & purification; D006801:Humans; D008969:Molecular Sequence Data; D010510:Periodontal Diseases / Q000276:immunology / Q000382:microbiology*
D000907:Antibodies, Bacterial; D006360:Heat-Shock Proteins