Webb J H, Mayer R J, Dixon L K
Institute for Animal Health, Pirbright Laboratory, Woking, UK.
FEBS Lett. 1999 Feb 5;444(1):136-9. doi: 10.1016/s0014-5793(99)00025-3.
An anti-ubiquitin cross-reactive protein which migrates more slowly (6.5 kDa) by SDS-PAGE than ubiquitin was identified in African swine fever virus particles. This protein was extracted into the detergent phase in Triton X-114 phase separations, showing that it is hydrophobic, and was radiolabelled with both [3H]palmitic acid and [32P]orthophosphate. This indicates that the protein has a similar structure to the membrane associated phosphatidyl ubiquitin described in baculovirus particles. A similar molecule was found in vaccinia virus and herpes simplex virus particles, suggesting that it may be a component of uninfected cell membranes, which is incorporated into membrane layers in virions during morphogenesis.
在非洲猪瘟病毒颗粒中鉴定出一种抗泛素交叉反应蛋白，在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）中其迁移速度比泛素慢（6.5 kDa）。该蛋白在Triton X-114相分离中被提取到去污剂相中，表明它具有疏水性，并且用[3H]棕榈酸和[32P]正磷酸盐进行了放射性标记。这表明该蛋白与杆状病毒颗粒中描述的膜相关磷脂酰泛素具有相似的结构。在痘苗病毒和单纯疱疹病毒颗粒中也发现了类似的分子，这表明它可能是未感染细胞膜的一个成分，在形态发生过程中被整合到病毒粒子的膜层中。
