改变棕榈酰化位点对流感病毒血凝素生物合成及功能的影响。
Effects of altering palmitylation sites on biosynthesis and function of the influenza virus hemagglutinin.
作者信息
Naim H Y, Amarneh B, Ktistakis N T, Roth M G
机构信息
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9038.
出版信息
J Virol. 1992 Dec;66(12):7585-8. doi: 10.1128/JVI.66.12.7585-7588.1992.
Abstract
Mutagenesis studies indicated that the three cytoplasmic cysteines of the influenza virus A/Japan/305/57 hemagglutinin (HA) are all palmitylated, but to an unequal extent. Replacement of all three cysteines abolished palmitylation, but affected neither HA biosynthesis nor function. Palmitate was not required for HA to be incorporated into virions.
摘要
诱变研究表明，甲型流感病毒A/日本/305/57血凝素（HA）的三个胞质半胱氨酸均被棕榈酰化，但程度不同。将所有三个半胱氨酸替换后消除了棕榈酰化，但既不影响HA的生物合成也不影响其功能。HA掺入病毒粒子并不需要棕榈酸酯。
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