Selective synthesis and secretion of particles composed of the hepatitis B virus middle surface protein directed by a recombinant vaccinia virus: induction of antibodies to pre-S and S epitopes.
Selective synthesis in mammalian cells of the hepatitis B virus middle surface (MS) protein, which is 55 amino acids longer than the major surface (S) protein, was achieved by using a recombinant vaccinia virus. The 33-kilodalton MS polypeptide was glycosylated and secreted as particles that resembled human hepatitis B surface antigen as well as particles composed solely of S protein with regard to antigenicity, buoyant density, size, and electron micrographic appearance. The MS particles differed from S particles, however, by binding to polymerized human albumin and inducing antibodies that reacted with a pre-S peptide and inhibited the binding of human plasma-derived hepatitis B surface antigen to polymerized human albumin.
D000818:Animals; D000917:Antibody Formation; D004274:DNA, Recombinant / Q000378:metabolism; D000939:Epitopes / Q000032:analysis*; D006514:Hepatitis B Surface Antigens / Q000276:immunology; D006515:Hepatitis B virus / Q000235:genetics* / Q000276:immunology; D007700:Kinetics; D008565:Membrane Proteins / Q000235:genetics*; D008970:Molecular Weight; D011817:Rabbits / Q000276:immunology; D014616:Vaccinia virus / Q000235:genetics* / Q000276:immunology; D014764:Viral Proteins / Q000235:genetics*
D004274:DNA, Recombinant; D000939:Epitopes; D006514:Hepatitis B Surface Antigens; D008565:Membrane Proteins; D014764:Viral Proteins