The role of disulfide bond isomerase A (DsbA) of Escherichia coli O157:H7 in biofilm formation and virulence

Yunho Lee; Younghoon Kim; Sujin Yeom; Saehun Kim; Sungsu Park; Che Ok Jeon; Woojun Park

doi:10.1111/j.1574-6968.2007.00993.x

The role of disulfide bond isomerase A (DsbA) of Escherichia coli O157:H7 in biofilm formation and virulence

Yunho Lee, Younghoon Kim, Sujin Yeom, Saehun Kim, Sungsu Park, Che Ok Jeon, Woojun Park

Research output: Contribution to journal › Article › peer-review

32 Citations (Scopus)

Abstract

The role of periplasmic disulfide oxidoreductase DsbA in Shiga toxin-producing Escherichia coli O157:H7 (STEC) was investigated. Deletion of dsbA (ΔdsbA) significantly decreased cell motility and alkaline phosphatase activity in STEC. STEC ΔdsbA also showed greater sensitivity to menadione and under low pH conditions. Significant reductions in surface attachment to both biotic (HT-29 epithelial cells) and abiotic (polystyrene and polyvinyl chloride) surfaces were observed in STEC ΔdsbA. In addition, no biofilm formation was detected in STEC ΔdsbA compared to wild-type cells in glass capillary tubes under continuous flow-culture system conditions. In the nematode model Caenorhabditis elegans-killing assay, the deletion of dsbA in STEC resulted in attenuated virulence compared to wild-type cells. STEC ΔdsbA was also found to have a reduced ability to colonize the nematode gut. These results suggest that DsbA plays important roles in biofilm formation and virulence in STEC cells.

Original language	English
Pages (from-to)	213-222
Number of pages	10
Journal	FEMS microbiology letters
Volume	278
Issue number	2
DOIs	https://doi.org/10.1111/j.1574-6968.2007.00993.x
Publication status	Published - 2008 Jan

Keywords

Biofilm
Caenorhabditis elegans
Disulfide bond
Virulence

ASJC Scopus subject areas

Medicine(all)

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10.1111/j.1574-6968.2007.00993.x

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title = "The role of disulfide bond isomerase A (DsbA) of Escherichia coli O157:H7 in biofilm formation and virulence",

abstract = "The role of periplasmic disulfide oxidoreductase DsbA in Shiga toxin-producing Escherichia coli O157:H7 (STEC) was investigated. Deletion of dsbA (ΔdsbA) significantly decreased cell motility and alkaline phosphatase activity in STEC. STEC ΔdsbA also showed greater sensitivity to menadione and under low pH conditions. Significant reductions in surface attachment to both biotic (HT-29 epithelial cells) and abiotic (polystyrene and polyvinyl chloride) surfaces were observed in STEC ΔdsbA. In addition, no biofilm formation was detected in STEC ΔdsbA compared to wild-type cells in glass capillary tubes under continuous flow-culture system conditions. In the nematode model Caenorhabditis elegans-killing assay, the deletion of dsbA in STEC resulted in attenuated virulence compared to wild-type cells. STEC ΔdsbA was also found to have a reduced ability to colonize the nematode gut. These results suggest that DsbA plays important roles in biofilm formation and virulence in STEC cells.",

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AU - Park, Sungsu

AU - Jeon, Che Ok

AU - Park, Woojun

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AB - The role of periplasmic disulfide oxidoreductase DsbA in Shiga toxin-producing Escherichia coli O157:H7 (STEC) was investigated. Deletion of dsbA (ΔdsbA) significantly decreased cell motility and alkaline phosphatase activity in STEC. STEC ΔdsbA also showed greater sensitivity to menadione and under low pH conditions. Significant reductions in surface attachment to both biotic (HT-29 epithelial cells) and abiotic (polystyrene and polyvinyl chloride) surfaces were observed in STEC ΔdsbA. In addition, no biofilm formation was detected in STEC ΔdsbA compared to wild-type cells in glass capillary tubes under continuous flow-culture system conditions. In the nematode model Caenorhabditis elegans-killing assay, the deletion of dsbA in STEC resulted in attenuated virulence compared to wild-type cells. STEC ΔdsbA was also found to have a reduced ability to colonize the nematode gut. These results suggest that DsbA plays important roles in biofilm formation and virulence in STEC cells.

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The role of disulfide bond isomerase A (DsbA) of Escherichia coli O157:H7 in biofilm formation and virulence

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