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甲型流感血凝素C末端锚定肽:鉴定与质谱研究。

Influenza A hemagglutinin C-terminal anchoring peptide: identification and mass spectrometric study.

作者信息

Kordyukova Larisa V, Ksenofontov Aleksander L, Serebryakova Marina V, Ovchinnikova Tatyana V, Fedorova Natalija V, Ivanova Valeria T, Baratova Ludmila A

机构信息

A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.

出版信息

Protein Pept Lett. 2004 Aug;11(4):385-91. doi: 10.2174/0929866043406850.

DOI:10.2174/0929866043406850
PMID:15327372
Abstract

MALDI-TOF MS and N-terminal amino acid sequencing allowed us to identify several fragments of the C-terminal peptide of Influenza A hemagglutinin (HA) containing transmembrane domains (TMD). These fragments were detected in the organic phase of chloroform-methanol extracts from bromelain-treated virus particles. Heterogeneous fatty acylation of the C-terminus was revealed. Tritium bombardment technique might open an opportunity for 3D structural investigation of the HA TMD in situ.

摘要

基质辅助激光解吸电离飞行时间质谱(MALDI-TOF MS)和N端氨基酸测序使我们能够鉴定出甲型流感血凝素(HA)含跨膜结构域(TMD)的C端肽的几个片段。这些片段在菠萝蛋白酶处理的病毒颗粒的氯仿-甲醇提取物的有机相中被检测到。揭示了C端的异质脂肪酰化。氚轰击技术可能为原位研究HA TMD的三维结构提供机会。

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Palmitoylation Contributes to Membrane Curvature in Influenza A Virus Assembly and Hemagglutinin-Mediated Membrane Fusion.
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J Virol. 2017 Oct 13;91(21). doi: 10.1128/JVI.00947-17. Print 2017 Nov 1.
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Site-specific S-acylation of influenza virus hemagglutinin: the location of the acylation site relative to the membrane border is the decisive factor for attachment of stearate.流感病毒血凝素的位点特异性S-酰化:酰化位点相对于膜边界的位置是硬脂酸附着的决定性因素。
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