METHODS: Here, the mechanism of LL-37 triggered changes in the structure and function of an enveloped virus is investigated. The bacteriophage \"Phi6\" is used as a surrogate for pathogenic enveloped viruses. Small angle X-ray and neutron scattering combined with light scattering techniques demonstrate that LL-37 actively integrates into the virus\'s lipid envelope.
RESULTS: LL-37 addition to Phi6 leads to curvature modification in the lipid bilayer, ultimately separating the envelope from the nucleocapsid. Additional biological assays confirm the loss of virus infectivity in the presence of LL-37, which coincides with the structural transformations. The results provide a fundamental understanding of the structure-activity relationship related to enveloped viruses. The knowledge of peptide-virus interactions can guide the design of future peptide-based antiviral drugs and therapies.
方法:这里,研究了LL-37触发包膜病毒结构和功能变化的机制。噬菌体“Phi6”用作致病性包膜病毒的替代品。小角度X射线和中子散射结合光散射技术表明LL-37主动整合到病毒的脂质包膜中。
结果:LL-37添加到Phi6导致脂质双层的曲率修饰,最终将包壳与核衣壳分开。另外的生物学测定证实了在LL-37存在下病毒感染性的丧失,这与结构转化一致。结果提供了与包膜病毒相关的结构-活性关系的基本理解。肽-病毒相互作用的知识可以指导未来基于肽的抗病毒药物和疗法的设计。