Characterization of a conformationally sensitive epitope on Moloney murine leukemia virus gp70.

We describe here several properties of a conformationally sensitive epitope common to the Moloney (M) and Rauscher (R) murine leukemia virus (MLV) gp70 family of glycoproteins, e.g., M-MLV gp70 and R-MLV gp71. This epitope was not detected by western blotting or by enzyme-linked immunosorbent assay experiments with three different lots of polyclonal R-MLV gp69/71 sera. However, it was detected when a specific monoclonal antibody, R47, was used in western blotting or immuno-dot-blotting experiments with the two viruses. R47 maps to a central 14-kd segment on R-MLV gp71 which spans an important structural domain, namely, that corresponding to the recombination site between ecotropic and endogenous envelope glycoprotein-coding sequences. Analysis of the western as well as dot blots developed with the R47 monoclonal antibody showed that about a 25-fold higher affinity for the epitope existed on R-MLV gp71, relative to M-MLV gp70. It thus appears that R-MLV and M-MLV gp70, although very closely related both structurally and serologically, are conformationally distinct in one domain, namely, the site of recombination between ecotropic and endogenous gp70-coding sequences.