Abstract
Physical association was measured between gp70, the envelope glycoprotein of Rauscher murine leukemia virus (R-MLV), and serologically defined H-2 antigens on the surface of R-MLV transformed C57BL/6 (H-2DbKb) mouse leukemia cells (RBL-5A). Capping and patching with antisera against H-2Db caused specific co-capping and co-patching of R-MLV gp70 antigens as seen by fluorescence microscopy. Despite the physical proximity of R-MLV gp70 and H-2Db antigens, high titer .alpha.R-MLV gp70 sera had no effect in blocking syngeneic T [thymus derived] lymphocyte-mediated cytolysis of RBL-5A cells, whereas .alpha.H-2Db sera were effective.