A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity

M P  Stevens; A  Friebel; L A  Taylor; M W  Wood; P J  Brown; W D  Hardt; E E  Galyov

doi:10.1128/JB.185.16.4992-4996.2003

A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity

M P Stevens, A Friebel, L A Taylor, M W Wood, P J Brown, W D Hardt, E E Galyov

Royal (Dick) School of Veterinary Studies

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

Abstract

We report the characterization of BopE, a type III secreted protein that is encoded adjacent to the Burkholderia pseudomallei bsa locus and is homologous to Salmonella enterica SopE/SopE2. Inactivation of bopE impaired bacterial entry into HeLa cells, indicating that BopE facilitates invasion. Consistent with this notion, BopE expressed in eukaryotic cells induced rearrangements in the subcortical actin cytoskeleton, and purified BopE exhibited guanine nucleotide exchange factor activity for Cdc42 and Rac1 in vitro.

Original language	English
Pages (from-to)	4992-4996
Number of pages	5
Journal	Journal of Bacteriology
Volume	185
Issue number	16
DOIs	https://doi.org/10.1128/JB.185.16.4992-4996.2003
Publication status	Published - Aug 2003

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10.1128/JB.185.16.4992-4996.2003

A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity
Copyright © 2003, American Society for Microbiology
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Stevens, M. P., Friebel, A., Taylor, L. A., Wood, M. W., Brown, P. J., Hardt, W. D., & Galyov, E. E. (2003). A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity. Journal of Bacteriology, 185(16), 4992-4996. https://doi.org/10.1128/JB.185.16.4992-4996.2003

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abstract = "We report the characterization of BopE, a type III secreted protein that is encoded adjacent to the Burkholderia pseudomallei bsa locus and is homologous to Salmonella enterica SopE/SopE2. Inactivation of bopE impaired bacterial entry into HeLa cells, indicating that BopE facilitates invasion. Consistent with this notion, BopE expressed in eukaryotic cells induced rearrangements in the subcortical actin cytoskeleton, and purified BopE exhibited guanine nucleotide exchange factor activity for Cdc42 and Rac1 in vitro.",

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AU - Stevens, M P

AU - Friebel, A

AU - Taylor, L A

AU - Wood, M W

AU - Brown, P J

AU - Hardt, W D

AU - Galyov, E E

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N2 - We report the characterization of BopE, a type III secreted protein that is encoded adjacent to the Burkholderia pseudomallei bsa locus and is homologous to Salmonella enterica SopE/SopE2. Inactivation of bopE impaired bacterial entry into HeLa cells, indicating that BopE facilitates invasion. Consistent with this notion, BopE expressed in eukaryotic cells induced rearrangements in the subcortical actin cytoskeleton, and purified BopE exhibited guanine nucleotide exchange factor activity for Cdc42 and Rac1 in vitro.

AB - We report the characterization of BopE, a type III secreted protein that is encoded adjacent to the Burkholderia pseudomallei bsa locus and is homologous to Salmonella enterica SopE/SopE2. Inactivation of bopE impaired bacterial entry into HeLa cells, indicating that BopE facilitates invasion. Consistent with this notion, BopE expressed in eukaryotic cells induced rearrangements in the subcortical actin cytoskeleton, and purified BopE exhibited guanine nucleotide exchange factor activity for Cdc42 and Rac1 in vitro.

UR - https://www.scopus.com/pages/publications/0041530031

U2 - 10.1128/JB.185.16.4992-4996.2003

DO - 10.1128/JB.185.16.4992-4996.2003

M3 - Article

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JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 16

ER -

A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity

Abstract

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