Neurath A R, Strick N
Lindsley F. Kimball Research Institute of the New York Blood Center, New York 10021.
Virology. 1994 Oct;204(1):475-7. doi: 10.1006/viro.1994.1558.
Annexin V and apolipoprotein H, reported to bind hepatitis B surface antigen (HBsAg) and presumed to react specifically with the HBsAg S protein and to play an important role in initiation of infection by hepatitis B virus, did not bind to delipidated HBsAg (dlHBsAg). Binding activity was restored by adding lipids to dlHBsAg. These results are consistent with the established affinity of annexin V and apolipoprotein H for lipids.
膜联蛋白V和载脂蛋白H据报道可结合乙型肝炎表面抗原(HBsAg),并推测与HBsAg S蛋白发生特异性反应,且在乙型肝炎病毒感染起始过程中发挥重要作用,但它们并不与脱脂HBsAg(dlHBsAg)结合。通过向dlHBsAg添加脂质可恢复结合活性。这些结果与膜联蛋白V和载脂蛋白H对脂质已确定的亲和力一致。