Yamaguchi M, Sugahara K, Shiosaki K, Mizokami H, Takeo K
Research Center for Pathogenic Fungi and Microbial Toxicoses, Chiba University, Japan.
FEMS Microbiol Lett. 1998 Aug 15;165(2):363-7. doi: 10.1111/j.1574-6968.1998.tb13171.x.
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.
利用高分辨率负染色、冰冻包埋及电子显微镜技术,对重组酵母细胞产生的乙型肝炎病毒表面抗原(HBsAg)颗粒的超微结构进行了检测。采用负染色法时,HBsAg颗粒呈球形至略呈卵形,平均直径为27.5纳米,由许多直径为4纳米的亚基组成。亚基上有一个微小的中央孔。采用冰冻包埋法时,颗粒大多呈球形至卵形,平均直径为23.7纳米,围绕电子半透明核心有一层7 - 8纳米厚的皮层。使用相同方法检测的人HBsAg颗粒较小,显然是由于多肽结构的分子差异。