An Aerolysin-like Pore-Forming Protein Complex Targets Viral Envelope to Inactivate Herpes Simplex Virus Type 1

Abstract Because most of animal viruses are enveloped, cytoplasmic entry these via fusion with cellular membrane initiates their invasion. However, the strategies in which host cells counteract such incompletely understood. Pore-forming toxin aerolysin-like proteins (ALPs) exist throughout kingdom, but functions mostly unknown. In this study, we report that βγ-crystallin fused protein and trefoil factor complex (βγ-CAT), an ALP from frog Bombina maxima, directly blocks enveloped virus invasion by interfering entry. βγ-CAT targeted acidic glycosphingolipids on HSV type 1 (HSV-1) envelope to induce pore formation, as indicated oligomer formation potassium calcium ion efflux. Meanwhile, formed ring-like oligomers ∼10 nm diameter liposomes induced dye release mimic viral envelope. Unexpectedly, transmission electron microscopy analysis showed βγ-CAT–treated HSV-1 was visibly intact vehicle-treated HSV-1, indicating did not lyse into HeLa totally hindered. vivo, topical application attenuated corneal infection mice. Collectively, results uncovered possesses capacity its featured antiviral-acting manner. Our findings will also largely help illustrate putative antiviral activity ALPs.