ASSOCIATION OF SOLUBLE MATRIX PROTEIN OF NEWCASTLE-DISEASE VIRUS WITH LIPOSOMES IS INDEPENDENT OF IONIC CONDITIONS
ASSOCIATION OF SOLUBLE MATRIX PROTEIN OF NEWCASTLE-DISEASE VIRUS WITH LIPOSOMES IS INDEPENDENT OF IONIC CONDITIONS
复制标题
DOI：
10.1016/0042-6822(88)90153-5
复制
发表时间：
1988-09-01
期刊：
影响因子：
3.7
通讯作者：
PEEPLES, ME
中科院分区：
文献类型：
--
作者：
FAABERG, KS;PEEPLES, ME
设计了一种纯化新城疫病毒可溶性基质(M)蛋白的免疫亲和方法。产生的M蛋白以小复合物的形式沉积在蔗糖梯度中。这种纯化的M蛋白与含有净中性、负电荷或正电荷的脂质体相关。脂质体由磷脂酰胆碱、胆固醇和提供电荷的第三种脂质组成。高盐条件不能阻止M蛋白与脂质体的结合。这些观察结果与M蛋白和脂质体之间的非静电关联一致。M蛋白三个独立表位的单克隆抗体均能结合M蛋白与脂质体的复合物，提示M蛋白三个表位不直接参与M蛋白与脂质体的相互作用。M蛋白还能够与缺乏胆固醇的脂质体结合，这意味着胆固醇在M蛋白-脂质体相互作用中并不起实质性作用。
An immunoaffinity method was designed for purification of a soluble form of the matrix (M) protein of Newcastle disease virus. The resulting M protein sedimented in a sucrose gradient as a small complex. This purified M protein associated with liposomes containing a net neutral, negative, or positive charge. The liposomes were composed of phosphatidylcholine, cholesterol, and a third lipid which provided the charge. The M protein-liposome associations were not prevented by high salt conditions. These observations are consistent with a nonelectrostatic association between the M protein and liposomes. Monoclonal antibodies to three separate epitopes of the M protein were all able to bind M protein complexed with liposomes, suggesting that the three M protein epitopes are not directly involved in the interaction between the M protein and liposomes. The M protein was also able to associate with liposomes lacking cholesterol implying that cholesterol does not play a substantial role in the M protein-liposome interaction.