Cleavage of host keratin 8 by a chlamydia-secreted protease
Cleavage of host keratin 8 by a chlamydia-secreted protease
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DOI：
10.1128/iai.72.7.3863-3868.2004
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发表时间：
2004-07-01
影响因子：
3.1
通讯作者：
Zhong, GM
中科院分区：
文献类型：
--
作者：
Dong, F;Su, H;Zhong, GM
在真核细胞中，衣原体必须在胞质空泡内复制。衣原体空泡的扩张是衣原体空泡内复制所必需的，而空泡内复制不可避免地引起宿主细胞骨架重排。在衣原体感染细胞的可溶性部分中检测到对应于中心杆区域的角蛋白8的裂解片段。由于角蛋白8是简单上皮细胞中中间丝的主要成分，角蛋白8的裂解可能增加宿主细胞骨架的溶解度，从而允许衣原体感染细胞中的空泡扩张。衣原体分泌的蛋白酶命名为CPAF（衣原体蛋白酶/蛋白酶体样活性因子）是必要的和足够的角蛋白8切割在衣原体感染的细胞，这表明衣原体已演变为修改宿主细胞骨架的特定机制。
Chlamydiae have to replicate within a cytoplasmic vacuole in eukaryotic cells. Expansion of the chlamydia-laden vacuole is essential for chlamydial intravacuolar replication, which inevitably causes host cell cytoskeleton rearrangements. A cleavage fragment of keratin 8 corresponding to the central rod region was detected in the soluble fraction of chlamydia-infected cells. Since keratin 8 is a major component of the intermediate filaments in simple epithelial cells, cleavage of keratin 8 may increase the solubility of the host cell cytoskeleton and thus permit vacuole expansion in chlamydia-infected cells. A chlamydia-secreted protease designated CPAF (chlamydial protease/proteasome-like activity factor) was both necessary and sufficient for keratin 8 cleavage in chlamydia-infected cells, suggesting that chlamydiae have evolved specific mechanisms for modifying the host cell cytoskeleton.