溶血磷脂酰胆碱可逆地阻止了多种病毒融合蛋白介导的合胞体形成过程中的孔道扩张。
Lysophosphatidylcholine reversibly arrests pore expansion during syncytium formation mediated by diverse viral fusogens.
机构信息
Department of Microbiology & Immunology, Dalhousie University, Halifax, Nova Scotia, Canada.
出版信息
J Virol. 2014 Jun;88(11):6528-31. doi: 10.1128/JVI.00314-14. Epub 2014 Mar 26.
Abstract
Using lysophosphatidylcholine, a curvature-inducing lysolipid, we have isolated a reversible, "stalled pore" phenotype during syncytium formation induced by the p14 fusion-associated small transmembrane (FAST) protein and influenza virus hemagglutinin (HA) fusogens. This is the first evidence that lateral propagation of stable fusion pores leading to syncytiogenesis mediated by diverse viral fusogens is inhibited by promotion of positive membrane curvature in the outer leaflets of the lipid bilayer surrounding intercellular fusion pores.
摘要
使用溶血磷脂酰胆碱，一种诱导曲率的溶血磷脂，我们在由 p14 融合相关小跨膜（FAST）蛋白和流感病毒血凝素（HA）融合蛋白诱导的合胞体形成过程中分离出一种可逆的“停滞孔”表型。这是第一个证据，表明由不同病毒融合蛋白介导的稳定融合孔的横向传播导致合胞体形成被促进脂质双层外层的正膜曲率的方式所抑制。
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