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) particles produced by recombinant yeast cells was examined using high-resolution negative staining, and ice embedding, electron microscopy. With negative 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 7-8 nm thick cortex surrounding an electron translucent core. Human HBsAg particles, examined using the same methods, were smaller, apparently because of molecular differences in polypeptide structure.
Yamaguchi
M
M
Research Center for Pathogenic Fungi and Microbial Toxicoses, Chiba University, Japan.
Sugahara
K
K
Shiosaki
K
K
Mizokami
H
H
Takeo
K
K
D004591:Electrophoresis, Polyacrylamide Gel; D006514:Hepatitis B Surface Antigens / Q000097:blood* / Q000737:chemistry / Q000302:isolation & purification / Q000648:ultrastructure*; D006801:Humans; D007053:Ice; D008854:Microscopy, Electron; D016624:Negative Staining; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism*; D016610:Tissue Embedding; D014614:Vaccines, Synthetic
D006514:Hepatitis B Surface Antigens; D007053:Ice; D014614:Vaccines, Synthetic