Topography of murine leukemia virus envelope proteins: characterization of transmembrane components

Abstract

Trypsinization of intact Moloney murine leukemia virus resulted in cleavage of p15(E) and Pr15(E) at a site near the middle of the molecule, producing a 9,000-dalton amino-terminal fragment which contains the disulfide linkage site to gp70 and which carries p15(E) epitopes b and c, but not epitope a. After solubilization of the viral membrane, trypsinization occurred at a second site within 1,000 daltons of the carboxy end of p15(E). This site is not exposed in intact virions, indicating that p15(E) and Pr15(E) are transmembrane proteins.