Open AccessFine structure of hepatitis B virus surface antigen produced by recombinant yeast: comparison with HBsAg of human origin
Author(s) -
Yamaguchi Masashi,
Sugahara Keishin,
Shiosaki Koichi,
Mizokami Hiroshi,
Takeo Kanji
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb13171.x
Subject(s) - hbsag , recombinant dna , virology , antigen , yeast , hepatitis b virus , virus , biology , microbiology and biotechnology , gene , immunology , biochemistry
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.