Association Of Hsp 70 And Gp96 With Immunogenic Peptide Antigens In Cells

Recently, several studies provided direct evidence that immunogenicity of stress protein preparations is due to bound peptides. Arnold et al. [60] showed that only gp96 preparations from TAP competent cells can induce CTL responses against antigens, whose presentation is TAP-dependent. In conclusion, gp96 can associate with CTL-recognized peptide antigens translocated by TAP. Further studies showed that the depletion of peptides from tumor-derived HSP 70 preparations abrogated their immunogenicity [37, 45, 61]. Two studies obtained direct evidence for the association of naturally processed CTL recognized peptide epitopes with HSP 70 and gp96 in cells. Nieland et al. reported the isolation of a naturally processed VSV-peptide epitope from gp96 preparations of VSV infected cells and Breloer et al. showed the isolation of naturally processed ovalbumin epitopes from gp96 and HSP 70 derived from ovalbumin transfected cells [62,63], We obtained experimental evidence that gp96 in human melanoma cells is associated with different CTL-recognized melanoma peptide antigens. In these experiments it was observed that HLA-A2 restricted CTL clones specific for different melanoma peptide antigens, especially for a tyrosinase peptide antigen, were preferentially stimulated by gp96 from the autologous melanoma cells in presence of APC [64],

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