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首页> 外文期刊>Infection and immunity >β1-Chain Integrins Are Not Essential for Intimin-Mediated Host Cell Attachment and EnteropathogenicEscherichia coli-Induced Actin Condensation
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β1-Chain Integrins Are Not Essential for Intimin-Mediated Host Cell Attachment and EnteropathogenicEscherichia coli-Induced Actin Condensation

机译:β1链整合素对内膜介导的宿主细胞附着和肠致病性大肠杆菌诱导的肌动蛋白凝集不是必需的

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Intimin is a bacterial outer membrane protein required for intimate attachment of enterohemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) to mammalian cells. β1-chain integrins have been proposed as candidate receptors for intimin. We found that binding of mammalian cells to immobilized intimin was not detectable unless mammalian cells were preinfected with EPEC or EHEC. β1-chain integrin antagonists or inactivation of the gene encoding the β1-chain did not affect binding of preinfected mammalian cells to intimin or the actin condensation associated with the attachment of EPEC. The results indicate that β1-chain integrins are not essential for intimin-mediated cell attachment or EPEC-mediated actin polymerization.
机译:内膜蛋白是一种细菌性外膜蛋白,可将肠出血性和肠致病性大肠杆菌(EHEC和EPEC)紧密附着在哺乳动物细胞上。 β 1 -链整合素已被提议作为内膜素的候选受体。我们发现,除非用EPEC或EHEC预先感染哺乳动物细胞,否则无法检测到哺乳动物细胞与固定的intimin的结合。 β 1 链整合素拮抗剂或β 1 链编码基因的失活不会影响预感染的哺乳动物细胞与内膜素的结合或与肌钙蛋白附着相关的肌动蛋白缩合。 EPEC。结果表明,β 1 链整合素对于内膜素介导的细胞粘附或EPEC介导的肌动蛋白聚合不是必需的。

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