The expression of mycobacterial heat shock protein (HSP64) on Meth A tumour cells.
Immunological cross-reactivity between Mycobacterium bovis BCG stress protein (heat shock protein: HSP64) and Meth A tumour cells was analysed by using anti-BCG HSP64 mAb whose recognition epitopes were characterized against BCG HSP64 peptides. By indirect immunofluorescence analysis (IIFA), it was found that one of seven anti-BCG HSP64 mAb, XVIIIG1, bound to the cell surface of Meth A in BALB/c mice. This result was further confirmed by western blot analysis, demonstrating the presence of a 64 kDa protein which reacted with mAb XVIIIG1 that recognizes the 110-123 amino acid peptide of the BCG HSP64. Comparison of the amino acid sequence between the mouse HSP65 and BCG HSP64 recognized by mAb XVIIIG1 revealed 50% amino acid sequence homology. It was concluded from these results that Meth A tumour cells continuously express the stress protein HSP64 as a kind of tumour-associated antigen on the surface of tumour cells.
Sasaki
J
J
Department of Bacteriology, Hirosaki University School of Medicine, Japan.
Dejehansart
M
M
De Bruyn
J
J
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000951:Antigens, Neoplasm / Q000276:immunology; D003429:Cross Reactions / Q000276:immunology; D000939:Epitopes / Q000276:immunology; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000276:immunology*; D051379:Mice; D008807:Mice, Inbred BALB C; D008819:Mice, Nude; D008969:Molecular Sequence Data; D009163:Mycobacterium bovis / Q000276:immunology*; D009374:Neoplasms, Experimental / Q000276:immunology*; D017386:Sequence Homology, Amino Acid; D014407:Tumor Cells, Cultured
D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D000939:Epitopes; D006360:Heat-Shock Proteins