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流感血凝素在内质网和中间区室中的折叠与寡聚化。

Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.

作者信息

Tatu U, Hammond C, Helenius A

机构信息

Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510, USA.

出版信息

EMBO J. 1995 Apr 3;14(7):1340-8. doi: 10.1002/j.1460-2075.1995.tb07120.x.

DOI:10.1002/j.1460-2075.1995.tb07120.x
PMID:7729412
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC398219/
Abstract

Influenza hemagglutinin (HA) was used to analyze the stepwise folding and oligomeric assembly of glycoproteins in the early secretory pathway of living cells. In addition to mature trimers, six distinct maturation intermediates were identified. Of these, all the incompletely oxidized forms were located in the endoplasmic reticulum (ER) and associated with calnexin, a membrane-bound, lectin-like ER chaperone. Once fully oxidized, the HA dissociated from calnexin as a monomer, which rapidly became resistant to dithiothreitol (DTT) reduction. Part of these extensively folded molecules moved as monomers into the intermediate compartment between the ER and the Golgi complex. Assembly of homotrimers occurred without calnexin-involvement within the ER and in the intermediate compartment. When anchor-free HA molecules were analyzed, it was found that they reach the DTT-resistant monomeric conformation but fail to trimerize. Taken together, the results provide a definition and intracellular localization of several intermediates in the conformational maturation of HA, including the immediate precursor for trimer assembly.

摘要

流感血凝素（HA）用于分析活细胞早期分泌途径中糖蛋白的逐步折叠和寡聚组装。除了成熟三聚体外，还鉴定出六种不同的成熟中间体。其中，所有未完全氧化的形式都位于内质网（ER）中，并与钙连蛋白相关，钙连蛋白是一种膜结合的、凝集素样的内质网伴侣蛋白。一旦完全氧化，HA作为单体从钙连蛋白上解离，迅速变得对二硫苏糖醇（DTT）还原具有抗性。这些广泛折叠的分子中的一部分以单体形式进入内质网和高尔基体复合体之间的中间区室。同三聚体的组装在内质网和中间区室内不涉及钙连蛋白的情况下发生。当分析无锚定HA分子时，发现它们达到了对DTT具有抗性的单体构象，但无法三聚化。综上所述，这些结果为HA构象成熟过程中几种中间体提供了定义和细胞内定位，包括三聚体组装的直接前体。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/d7ea9cc8a817/emboj00031-0071-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/203a7831d513/emboj00031-0065-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/01585d2ec15f/emboj00031-0066-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/896fd1fbb8d3/emboj00031-0067-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/92d919720dc1/emboj00031-0068-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/fc16baf61f86/emboj00031-0069-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/d736967b2bcb/emboj00031-0070-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/d7ea9cc8a817/emboj00031-0071-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/203a7831d513/emboj00031-0065-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/01585d2ec15f/emboj00031-0066-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/896fd1fbb8d3/emboj00031-0067-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/92d919720dc1/emboj00031-0068-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/fc16baf61f86/emboj00031-0069-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/d736967b2bcb/emboj00031-0070-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a04f/398219/d7ea9cc8a817/emboj00031-0071-a.jpg

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