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Volume 158, Issue 11

Absence of O antigen suppresses IcsA autochaperone region mutations Free

Abstract

The IcsA (VirG) protein is a polarly distributed autotransporter protein. IcsA functions as a virulence factor by interacting with the host actin regulatory protein N-WASP, which in turn activates the Arp2/3 complex, initiating actin polymerization. Formation of F-actin comet tails allows bacterial cell-to-cell spreading. Although various accessory proteins such as periplasmic chaperones and the β-barrel assembly machine (BAM) complex have been shown to be involved in the export of IcsA, the IcsA translocation mechanism remains to be fully elucidated. A putative autochaperone (AC) region (amino acids 634–735) located at the C-terminal end of the IcsA passenger domain, which forms part of the self-associating autotransporter (SAAT) domain, has been suggested to be required for IcsA biogenesis, as well as for N-WASP recruitment, based on mutagenesis studies. IcsA proteins with linker insertion mutations within the AC region have a significant reduction in production and are defective in N-WASP recruitment when expressed in smooth LPS (S-LPS) . In this study, we have found that the LPS O antigen plays a role in IcsA production based on the use of an () mutant having rough LPS (R-LPS) and a novel assay in which O antigen is depleted using tunicamycin treatment and then regenerated. In addition, we have identified a new N-WASP binding/interaction site within the IcsA AC region.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Funding
This study was supported by the:
  • National Health and Medical Research Council
  • NHMRC
  • University of Adelaide
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2012-11-01
2024-04-28
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Absence of O antigen suppresses Shigella flexneri IcsA autochaperone region mutations
Microbiology 158, 2835 (2012); https://doi.org/10.1099/mic.0.062471-0
/content/journal/micro/10.1099/mic.0.062471-0
/content/journal/micro/10.1099/mic.0.062471-0
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