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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.

DOI:10.1128/JVI.66.12.7585-7588.1992
PMID:1433532
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC240475/
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。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df7f/240475/3987e9cbedce/jvirol00043-0763-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df7f/240475/6a93b83d52be/jvirol00043-0762-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df7f/240475/3987e9cbedce/jvirol00043-0763-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df7f/240475/6a93b83d52be/jvirol00043-0762-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df7f/240475/3987e9cbedce/jvirol00043-0763-a.jpg

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本文引用的文献

1
Physiological characterization of influenza virus temperature-sensitive mutants defective in the haemagglutinin gene.血凝素基因缺陷的流感病毒温度敏感突变体的生理学特性
J Gen Virol. 1984 Nov;65 ( Pt 11):1889-97. doi: 10.1099/0022-1317-65-11-1889.
2
Mutations in the cytoplasmic domain of the influenza virus hemagglutinin affect different stages of intracellular transport.流感病毒血凝素胞质结构域中的突变会影响细胞内运输的不同阶段。
J Cell Biol. 1985 Mar;100(3):704-14. doi: 10.1083/jcb.100.3.704.
3
The J.D. mutation in familial hypercholesterolemia: amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors.
Protein Cell. 2016 Jan;7(1):28-45. doi: 10.1007/s13238-015-0193-x. Epub 2015 Jul 28.
4
Palmitoylation of virus proteins.病毒蛋白的棕榈酰化。
Biol Cell. 2012 Sep;104(9):493-515. doi: 10.1111/boc.201200006. Epub 2012 Jul 17.
5
Association of influenza virus proteins with membrane rafts.流感病毒蛋白与膜筏的关联。
Adv Virol. 2011;2011:370606. doi: 10.1155/2011/370606. Epub 2011 Jul 25.
6
S acylation of the hemagglutinin of influenza viruses: mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine.流感病毒血凝素的硬脂酰化：质谱分析揭示硬脂酸在跨膜半胱氨酸上的位点特异性附着。
J Virol. 2008 Sep;82(18):9288-92. doi: 10.1128/JVI.00704-08. Epub 2008 Jul 2.
7
The carboxy-terminal domain of glycoprotein N of human cytomegalovirus is required for virion morphogenesis.人巨细胞病毒糖蛋白N的羧基末端结构域是病毒体形态发生所必需的。
J Virol. 2007 May;81(10):5212-24. doi: 10.1128/JVI.01463-06. Epub 2007 Jan 17.
8
Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion.严重急性呼吸综合征冠状病毒刺突糖蛋白富含半胱氨酸的胞内区域的棕榈酰化对于刺突介导的细胞融合很重要。
Virology. 2007 Apr 10;360(2):264-74. doi: 10.1016/j.virol.2006.10.034. Epub 2006 Nov 28.
9
Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly.流感病毒血凝素（H3亚型）组装需要其胞质尾的棕榈酰化：两种亚型的M1蛋白在支持组装的能力上有所不同。
J Virol. 2005 Nov;79(21):13673-84. doi: 10.1128/JVI.79.21.13673-13684.2005.
10
Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity.酰化介导的禽流感病毒血凝素膜锚定对于融合孔形成和病毒感染性至关重要。
J Virol. 2005 May;79(10):6449-58. doi: 10.1128/JVI.79.10.6449-6458.2005.
家族性高胆固醇血症中的J.D.突变：细胞质结构域中的氨基酸取代阻碍低密度脂蛋白受体的内化。
Cell. 1986 Apr 11;45(1):15-24. doi: 10.1016/0092-8674(86)90533-7.
4
Rapid and efficient site-specific mutagenesis without phenotypic selection.无需表型筛选的快速高效位点特异性诱变。
Proc Natl Acad Sci U S A. 1985 Jan;82(2):488-92. doi: 10.1073/pnas.82.2.488.
5
Deletion of the cytoplasmic domain of the polymeric immunoglobulin receptor prevents basolateral localization and endocytosis.多聚免疫球蛋白受体胞质结构域的缺失会阻止其基底外侧定位和内吞作用。
Cell. 1986 Nov 7;47(3):359-64. doi: 10.1016/0092-8674(86)90592-1.
6
The structure and function of the hemagglutinin membrane glycoprotein of influenza virus.流感病毒血凝素膜糖蛋白的结构与功能
Annu Rev Biochem. 1987;56:365-94. doi: 10.1146/annurev.bi.56.070187.002053.
7
Heterologous transmembrane and cytoplasmic domains direct functional chimeric influenza virus hemagglutinins into the endocytic pathway.异源跨膜和细胞质结构域将功能性嵌合流感病毒血凝素导向内吞途径。
J Cell Biol. 1986 Apr;102(4):1271-83. doi: 10.1083/jcb.102.4.1271.
8
A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits.细胞质结构域中的单个氨基酸变化使得流感病毒血凝素能够通过有被小窝进行内吞作用。
Cell. 1988 Jun 3;53(5):743-52. doi: 10.1016/0092-8674(88)90092-x.
9
Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant.水泡性口炎病毒糖蛋白突变体拯救所需的糖蛋白胞质结构域序列
J Virol. 1989 Sep;63(9):3569-78. doi: 10.1128/JVI.63.9.3569-3578.1989.
10
The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin.
J Biol Chem. 1990 Mar 15;265(8):4760-7.