FINE-STRUCTURE OF HEPATITIS-B VIRUS SURFACE-ANTIGEN PRODUCED BY RECOMBINANT YEAST - COMPARISON WITH HBSAG OF HUMAN-ORIGIN

The ultrastructure of hepatitis B virus surface antigen (HBsAg) partic les produced by recombinant yeast cells was examined using high-resolu tion negative staining, and ice embedding; electron microscopy. With n egative staining, the HBsAg particles were spherical to slightly ovoid with a mean diameter of 27.5 nm and consisted of many subunits each 4 nm in diameter. Subunits were marked with a minute central pore. With ice embedding, particles were mostly spherical to ovoid, with a mean diameter of 23.7 nm and a 7-5 nm thick cortex surrounding an electron translucent core. Human HBsAg particles, examined using the same metho ds, were smaller, apparently because of molecular differences in polyp eptide structure. (C) 1998 Federation of European Microbiological Soci eties. Published by Elsevier Science B.V. All rights reserved.