Phospholipid interactions of the putative fusion peptide of hepatitis B virus surface antigen S protein.
Phospholipid interactions of the putative fusion peptide of hepatitis B virus surface antigen S protein.
复制标题
乙型肝炎病毒表面抗原 S 蛋白的假定融合肽的磷脂相互作用。
DOI：
10.1099/0022-1317-76-2-301
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Gavilanes,F
中科院分区：
文献类型：
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作者：
Rodriguez-Crespo,I;Nunez,E;Gomez-Gutierrez,J;Yelamos,B;Albar,JP;Peterson,DL;Gavilanes,F
包膜病毒感染周期的第一步是病毒与细胞膜的融合。这一过程通常是由于位于病毒包膜糖蛋白氨基末端的病毒融合肽导致膜不稳定而实现的。Rodriguez-Crespoet等人（Journal of General virology, 75,637 - 639,1994）先前的序列相似性研究表明，乙型肝炎病毒S蛋白氨基末端序列的疏水链段与逆转录病毒和副粘病毒的融合肽具有一些相同的特征。合成了具有该序列的16残基肽，并对其与脂质体的相互作用进行了表征。在3.5 ~ 52.0µm的浓度范围内，该肽能够以pH依赖的方式介导囊泡聚集、脂质混合和脂质体泄漏。这些作用仅针对带负电荷的磷脂囊泡。这种肽还能使红细胞溶血。这项研究支持了这样一种观点，即该序列可能在该病毒的初始感染步骤中很重要，与靶膜相互作用并导致其随后的不稳定。
One of the first steps in the infective cycle of an enveloped virus consists of the fusion of the viral and cellular membranes. This process is usually achieved as a result of membrane destabilization brought about by a viral fusion peptide located at the amino terminus of one of the viral envelope glycoproteins. Previous sequence similarity studies by Rodriguez-Crespoet al. (Journal of General Virology75, 637–639, 1994) have shown that a hydrophobic stretch in the amino-terminal sequence of the S protein of hepatitis B virus shares several characteristics with fusion peptides of retroviruses and paramyxoviruses. A 16 residue peptide with this sequence was synthesized and its interaction with liposomes characterized. This peptide was able to mediate vesicle aggregation, lipid mixing and liposome leakage in a pH dependent manner at concentrations ranging from 3.5 to 52.0 µm. These effects were specific for negatively charged phospholipid vesicles. The peptide was also able to haemolyse erythrocytes. This study supports the notion that the sequence might be important in the initial infective steps of this virus, interacting with the target membranes and bringing about their subsequent destabilization.