Stress-induced proteins may have significant roles in anti-tumor resistance. To clarify the immunobiological roles of these proteins, we first developed monoclonal antibody (mAb) H1A that detects the HeLa cell-surface antigens whose expression was enhanced by treatment of the cells with physico-chemical stressors, such as heat, H2O2 and tumor necrosis factor. H1A (IgM) detects several molecules with mol. wt. 30, 43, 75, 90, 100, 120 and 150 kDa in Western blot analysis of HeLa cell lysates. Although the antigen was constitutively expressed on the HeLa cell surface, the cell-surface expression of H1A-defined antigen was rapidly enhanced (within 1 h) after heat treatment of HeLa cells. H1A antigens were also transformation-associated, since 1) the activated oncogene-transformed fibroblasts expressed the antigens, but parental nontransformed cells did not, and 2) certain human neoplastic but not normal cells strongly expressed the antigens. Furthermore, H1A mAb also partly blocked the cytotoxicity of purified protein derivatives-stimulated human T cell receptor gamma delta-type T cells towards HeLa cells. Taken together, these data indicate that H1A-defined stress-inducible proteins may play a vital role in anti-tumor resistance by cytotoxic T cells.