Abstract:
:IcsA is an outer membrane protein in the autotransporter family that is required for Shigella flexneri pathogenesis. Following its secretion through the Sec translocon, IcsA is incorporated into the outer membrane in a process that depends on YaeT, a component of an outer membrane beta-barrel insertion machinery. We investigated the role of the periplasmic chaperone Skp in IcsA maturation. Skp is required for the presentation of the mature amino terminus (alpha-domain) of IcsA on the bacterial surface and contributes to cell-to-cell spread of S. flexneri in cell culture. A mutation in skp does not prevent the insertion of the beta-barrel into the outer membrane, suggesting that the primary role of Skp is the folding of the IcsA alpha-domain. In addition, the requirement for skp can be partially bypassed by disrupting icsP, an ortholog of Escherichia coli ompT, which encodes the protease that processes IcsA between the mature amino terminus and the beta-barrel outer membrane anchor. These findings are consistent with a model in which Skp plays a critical role in the chaperoning of the alpha-domain of IcsA during transit through the periplasm.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Wagner JK,Heindl JE,Gray AN,Jain S,Goldberg MBdoi
10.1128/JB.00989-08subject
Has Abstractpub_date
2009-02-01 00:00:00pages
815-21issue
3eissn
0021-9193issn
1098-5530pii
JB.00989-08journal_volume
191pub_type
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journal_title:Journal of bacteriology
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pub_type: 杂志文章
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更新日期:1962-02-01 00:00:00
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pub_type: 杂志文章
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更新日期:1978-07-01 00:00:00