Schroth B, Philipp H C, Veit M, Schmidt M F, Herrmann A
Institut für Biologie und Biophysik, Mathematisch-Naturwissenschaftliche Fakulrät I. Humboldt-Universität zu Berlin, Germany.
Pflugers Arch. 1996;431(6 Suppl 2):R257-8. doi: 10.1007/BF02346366.
The relevance of palmitoylation of cysteine residues of influenza virus hemagglutinin (HA) for the HA-mediated membrane fusion triggered at low pH is investigated. Either wild-type HA (subtype H7) or mutant HA devoid of fatty acids were expressed in insect cells. The kinetics as well as the extent of fusion of HA-expressing cells with human erythrocyte ghosts were measured by a membrane mixing assay. Fusion was measured continuously at different pH by fluorescence dequenching of the lipid-like fluorophore R18 initially incorporated into the erythrocyte membrane. No significant difference between fusion of wild-type and mutant HA expressing cells with ghosts could be detected showing that deacylation does affect neither the extent nor the kinetics of fusion.
研究了流感病毒血凝素（HA）半胱氨酸残基的棕榈酰化与低pH触发的HA介导的膜融合的相关性。野生型HA（H7亚型）或不含脂肪酸的突变型HA在昆虫细胞中表达。通过膜混合试验测量表达HA的细胞与人红细胞空壳融合的动力学以及融合程度。通过最初掺入红细胞膜中的类脂荧光团R18的荧光猝灭，在不同pH下连续测量融合。未检测到野生型和突变型HA表达细胞与空壳融合之间的显著差异，表明去酰化既不影响融合程度也不影响融合动力学。
