Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide
Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide
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DOI：
10.1128/jvi.00415-08
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发表时间：
2008-09-01
影响因子：
5.4
通讯作者：
Rottier, Peter J. M.
中科院分区：
文献类型：
--
作者：
Bosch, Berend Jan;Bartelink, Willem;Rottier, Peter J. M.
与其他I类病毒融合蛋白不同，严重急性呼吸道综合征冠状病毒粒子上的刺突蛋白是未切割的。正如我们和其他人所证明的，这种病毒的感染依赖于靶细胞内体区室中存在的组织蛋白酶，这表明刺突蛋白在细胞进入期间而不是在病毒体生物发生期间通过切割获得其融合能力。在这里，我们证明，组织蛋白酶L确实激活纤突蛋白的膜融合功能。此外，切割被映射到相同的区域，在冠状病毒携带弗林蛋白酶激活的刺突，蛋白质的受体结合亚基从膜锚定的融合亚基分离。
Unlike other class I viral fusion proteins, spike proteins on severe acute respiratory sydrome coronavirus virions are uncleaved. As we and others have demonstrated, infection by this virus depends on cathepsin proteases present in endosomal compartments of the target cell, suggesting that the spike protein acquires its fusion competence by cleavage during cell entry rather than during virion biogenesis. Here we demonstrate that cathepsin L indeed activates the membrane fusion function of the spike protein. Moreover, cleavage was mapped to the same region where, in coronaviruses carrying furin-activated spikes, the receptor binding subunit of the protein is separated from the membrane-anchored fusion subunit.