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麻疹病毒与膜辅因子蛋白（CD46）的结合：二硫键和N-聚糖对受体功能的重要性

Binding of measles virus to membrane cofactor protein (CD46): importance of disulfide bonds and N-glycans for the receptor function.

作者信息

Maisner A, Schneider-Schaulies J, Liszewski M K, Atkinson J P, Herrler G

机构信息

Institut für Virologie, Philipps-Universität Marburg, Germany.

出版信息

J Virol. 1994 Oct;68(10):6299-304. doi: 10.1128/JVI.68.10.6299-6304.1994.

DOI:10.1128/JVI.68.10.6299-6304.1994
PMID:8083969
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC237050/
Abstract

Two cellular proteins, membrane cofactor protein (MCP) and moesin, were reported recently to be functionally associated with the initiation of a measles virus infection. We have analyzed the interaction of measles virus with cell surface proteins, using an overlay binding assay with cellular proteins immobilized on nitrocellulose. Among surface-biotinylated proteins from a human rectal tumor cell line (HRT), measles virus was able to bind only to a 67-kDa protein that was identified as MCP. The virus recognized different isoforms of MCP expressed from human (HRT and HeLa) and simian (Vero) cell lines. The binding of measles virus to MCP was abolished after cleavage of the disulfide bonds by reducing agents as well as after enzymatic release of N-linked oligosaccharides. By contrast, removal of sialic acid or O-linked oligosaccharides did not affect the recognition of MCP measles virus. These data indicate that the receptor determinant of MCP is dependent on a conformation of the protein that is maintained by disulfide bonds and N-glycans present in the complement binding domains. Our results are consistent with a role of MCP as primary attachment site for measles virus in the initial stage of an infection. The functional relationship between MCP and moesin in a measles virus infection is discussed.

摘要

最近有报道称，两种细胞蛋白，即膜辅因子蛋白（MCP）和埃兹蛋白，在功能上与麻疹病毒感染的起始相关。我们使用固定在硝酸纤维素上的细胞蛋白进行覆盖结合试验，分析了麻疹病毒与细胞表面蛋白的相互作用。在来自人直肠肿瘤细胞系（HRT）的表面生物素化蛋白中，麻疹病毒仅能与一种被鉴定为MCP的67 kDa蛋白结合。该病毒识别从人（HRT和HeLa）和猴（Vero）细胞系表达的不同MCP异构体。在用还原剂裂解二硫键后以及在N-连接寡糖酶促释放后，麻疹病毒与MCP的结合被消除。相比之下，去除唾液酸或O-连接寡糖并不影响麻疹病毒对MCP的识别。这些数据表明，MCP的受体决定簇取决于由补体结合域中存在的二硫键和N-聚糖维持的蛋白质构象。我们的结果与MCP作为麻疹病毒在感染初始阶段的主要附着位点的作用一致。本文还讨论了MCP和埃兹蛋白在麻疹病毒感染中的功能关系。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/5e51b5ba8ff8/jvirol00019-0178-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/9ff88bd19691/jvirol00019-0177-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/03f7e13bd682/jvirol00019-0177-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/f8e3c651bd17/jvirol00019-0178-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/56ceb7c74986/jvirol00019-0178-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/7089225f2419/jvirol00019-0178-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/5e51b5ba8ff8/jvirol00019-0178-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/9ff88bd19691/jvirol00019-0177-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/03f7e13bd682/jvirol00019-0177-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/f8e3c651bd17/jvirol00019-0178-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/56ceb7c74986/jvirol00019-0178-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/7089225f2419/jvirol00019-0178-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f5/237050/5e51b5ba8ff8/jvirol00019-0178-d.jpg

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本文引用的文献

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J Gen Virol. 1993 Jun;74 ( Pt 6):1073-9. doi: 10.1099/0022-1317-74-6-1073.
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The human CD46 molecule is a receptor for measles virus (Edmonston strain).人类CD46分子是麻疹病毒（埃德蒙斯顿株）的受体。
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Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus.人膜辅因子蛋白（CD46）作为麻疹病毒的细胞受体。
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The distal short consensus repeats 1 and 2 of the membrane cofactor protein CD46 and their distance from the cell membrane determine productive entry of species B adenovirus serotype 35.膜辅因子蛋白CD46的远端短共有重复序列1和2及其与细胞膜的距离决定了B种35型腺病毒的有效进入。
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Changes in the receptorbinding haemagglutinin protein of wild-type morbilliviruses are not required for adaptation to Vero cells.野生型麻疹病毒适应Vero细胞并不需要其受体结合血凝素蛋白发生变化。
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