کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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3424827 | 1227249 | 2010 | 8 صفحه PDF | دانلود رایگان |
Adenovirus disrupts endosomal membranes during cell entry. The membrane lytic capsid protein VI (pVI) facilitates entry by fragmenting membranes. Although an N-terminal amphipathic α-helix (VI-Φ) possesses similar membrane affinity as pVI, truncated protein lacking VI-Φ (VIΔ54) still possesses moderate membrane affinity. We demonstrate that incorporation of nickel–NTA lipids in membranes enhances the membrane affinity and the membrane lytic activity of VIΔ54. We also demonstrate that 3 predicted pVI α-helices within residues 54–114 associate with membranes, sitting roughly parallel to the membrane surface. His-tagged VIΔ54 is capable of fragmenting membranes similar to pVI and the VI-Φ peptide. Interestingly, neither VI-Φ nor His-tagged VIΔ54 can induce tubule formation in giant lipid vesicles as observed for pVI. These data suggest cooperativity between the amphipathic α-helix and residues in VIΔ54 to induce positive membrane curvature and tubule formation. These results provide additional details regarding the mechanism of nonenveloped virus membrane penetration.
Journal: Virology - Volume 408, Issue 1, 5 December 2010, Pages 31–38