Abstract：
OBJECTIVE: Enveloped viruses are pivotal in causing various illnesses, including influenza and COVID-19. The antimicrobial peptide LL-37, a critical part of the human innate immune system, exhibits potential as an antiviral agent capable of thwarting these viral threats. Its mode of action involves versatile and non-specific interactions that culminate in dismantling the viral envelope, ultimately rendering the viruses inert. However, the exact mechanism of action is not yet understood.
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.
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.
摘要：
目的：包膜病毒是引起各种疾病的关键，包括流感和COVID-19。抗菌肽LL-37，人类先天免疫系统的关键部分，表现出作为能够阻止这些病毒威胁的抗病毒剂的潜力。它的作用方式涉及多种和非特异性的相互作用，最终导致病毒包膜的解体，最终使病毒变得惰性。然而,确切的作用机制尚不清楚。
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。
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。
