Pinkenburg Olaf, Meyer Torben, Bannert Norbert, Norley Steven, Bolte Kathrin, Czudai-Matwich Volker, Herold Susanne, Gessner André, Schnare Markus
Institute for Immunology, Philipps-University of Marburg, Marburg, Germany.
Department for HIV and other Retroviruses, Robert Koch Institute, Berlin, Germany.
PLoS One. 2016 Jun 6;11(6):e0156929. doi: 10.1371/journal.pone.0156929. eCollection 2016.
In addition to their well-known antibacterial activity some antimicrobial peptides and proteins (AMPs) display also antiviral effects. A 27 aa peptide from the N-terminal part of human bactericidal/permeability-increasing protein (BPI) previously shown to harbour antibacterial activity inhibits the infectivity of multiple Influenza A virus strains (H1N1, H3N2 and H5N1) the causing agent of the Influenza pneumonia. In contrast, the homologous murine BPI-peptide did not show activity against Influenza A virus. In addition human BPI-peptide inhibits the activation of immune cells mediated by Influenza A virus. By changing the human BPI-peptide to the sequence of the mouse homologous peptide the antiviral activity was completely abolished. Furthermore, the human BPI-peptide also inhibited the pathogenicity of the Vesicular Stomatitis Virus but failed to interfere with HIV and measles virus. Electron microscopy indicate that the human BPI-peptide interferes with the virus envelope and at high concentrations was able to destroy the particles completely.
除了其众所周知的抗菌活性外,一些抗菌肽和蛋白质(AMPs)还具有抗病毒作用。先前已证明人杀菌/通透性增加蛋白(BPI)N端部分的一个27个氨基酸的肽具有抗菌活性,它能抑制多种甲型流感病毒株(H1N1、H3N2和H5N1)的感染性,这些病毒是流感肺炎的致病原。相比之下,同源的鼠源BPI肽对甲型流感病毒没有活性。此外,人BPI肽可抑制甲型流感病毒介导的免疫细胞激活。将人BPI肽的序列改变为小鼠同源肽的序列后,抗病毒活性完全丧失。此外,人BPI肽还抑制水疱性口炎病毒的致病性,但未能干扰HIV和麻疹病毒。电子显微镜显示,人BPI肽会干扰病毒包膜,在高浓度下能够完全破坏病毒颗粒。