title: Measurement of binding specificity between T cell lymphomas and murine leukemia viruses.
abstract: We have previously reported the presence of receptors on radiation leukemia virus (RadLV)-induced thymomas and malignant thymocytes from AKR mice which specifically bind retrovirus produced by these T cell clones. These receptors have been shown to have specificity for virus reminiscent of an immune-specific receptor. Previous studies on T cell lymphoma binding to retroviruses have involved measurement of the interaction of labelled virus with cells using fluorescence-activated cell sorter (FACS) analysis (McGrath et al., J. Virol. (1978) 25, 923; McGrath and Weissman, Cell (1979) 17, 65; Weissman and McGrath, Curr. Top. Microbiol. Immunol. (1982) 98, 103). Here we report development of an assay for measuring lymphoma binding to virus, prepared as an immunoabsorbent adhered to a microtiter plate. Using this assay, we have shown that only T and not B cell lymphomas can bind to T cell-tropic viruses, and some cell lines have greatest specificity for homologous virus. The AKR-derived T cell lymphomas, SL3 and KKT-2, show greater specificity for leukemogenic AKR viruses, than for an AKR xenotropic virus or the recombinant AKR virus, MCF247. The RadLV-induced T cell lines, C6VL/1 and BL/VL3, have been found to bind cross-reactively to several different murine leukemia viruses (MuLVs). RadLV-induced T cell lymphomas do have greater specificity for their cognate retroviruses since free, homologous retrovirus can best block the interaction between cells and virus adhered to the wells of a microtiter plate. Cross-reactive interactions are more easily demonstrated by this assay, probably because low avidity interactions are stabilized as a result of the mode of virus presentation. Binding specificity for retroviral envelope determinants has been demonstrated using a rat anti-retroviral antiserum prepared as an F(ab)1 fragment. This antiserum can inhibit the interaction between the C6VL/1 thymoma and its RadLV virus. Specificity of this antibody for a gp70-like protein was confirmed by NaDodSO4-polyacrylamide gel electrophoresis (PAGE) and by loss of this activity after absorption of antibody on virus. Antibodies specific for RadLV/VL3 gp70 determinants can inhibit the interaction of C6VL/1 with RadLV/VL3 suggesting that cross-reactive binding to heterologous virus is also specific for a gp70 viral env determinant.
authors.affiliation: Department of Pathology, Stanford University Medical Centre, CA 94305.
authors.forename: H C
authors.initials: HC
authors.lastname: O'Neill
authors.forename: I L
authors.initials: IL
authors.lastname: Weissman
mesh_terms: D000818:Animals; D007163:Immunosorbent Techniques; D009052:Leukemia Virus, Murine / Q000032:analysis / Q000276:immunology* / Q000378:metabolism; D008223:Lymphoma / Q000382:microbiology*; D051379:Mice; D009381:Neoplasms, Radiation-Induced / Q000382:microbiology*; D011991:Receptors, Virus / Q000378:metabolism*; D013601:T-Lymphocytes / Q000378:metabolism / Q000382:microbiology*; D013945:Thymoma / Q000382:microbiology*; D014407:Tumor Cells, Cultured; D014759:Viral Envelope Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000032:analysis
chemical_list: D011991:Receptors, Virus; D014759:Viral Envelope Proteins; D014764:Viral Proteins