Wharton S A, Martin S R, Ruigrok R W, Skehel J J, Wiley D C
National Institute for Medical Research, The Ridgeway, Mill Hill, London, U.K.
J Gen Virol. 1988 Aug;69 ( Pt 8):1847-57. doi: 10.1099/0022-1317-69-8-1847.
We have studied the interactions of synthetic peptides corresponding to the sequence of the amino terminus of the HA2 subunit of influenza virus haemagglutinin with artificial lipid membranes. The peptides could fuse cholesterol-free liposomes at neutral as well as acid pH; however, liposomes containing cholesterol could only be fused below pH 6. The fusion process caused leakage of aqueous liposomal contents. Peptides with amino acid substitutions had fusion properties similar to whole haemagglutinin molecules with the corresponding sequence changes. Non-fusogenic peptides still interacted with the membrane but did not cause leakage of liposomal contents. A correlation between the alpha-helical content of peptide and its fusogenicity was noted, but this was not absolute. The results reported here support suggestions for a role of the amino terminus of HA2 in virus-endosome fusion.
我们研究了与流感病毒血凝素HA2亚基氨基末端序列对应的合成肽与人工脂质膜的相互作用。这些肽在中性和酸性pH条件下都能使不含胆固醇的脂质体融合；然而，含有胆固醇的脂质体只能在pH 6以下融合。融合过程导致脂质体内容物泄漏。具有氨基酸替代的肽具有与具有相应序列变化的完整血凝素分子相似的融合特性。非融合肽仍与膜相互作用，但不会导致脂质体内容物泄漏。注意到肽的α-螺旋含量与其融合性之间存在相关性，但这并非绝对。此处报道的结果支持了HA2氨基末端在病毒-内体融合中起作用的观点。
