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The LapG protein plays a role in Pseudomonas aeruginosa biofilm formation by controlling the presence of the CdrA adhesin on the cell surface

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Rybtke, Morten ; Berthelsen, Jens ; Yang, Liang ; Høiby, Niels ; Givskov, Michael ; Tolker-Nielsen, Tim. / The LapG protein plays a role in Pseudomonas aeruginosa biofilm formation by controlling the presence of the CdrA adhesin on the cell surface. I: MicrobiologyOpen. 2015 ; Bind 4, Nr. 6. s. 917-30.

Bibtex

@article{e67ede5daf3d4631ac9d68da7c8ddc70,
title = "The LapG protein plays a role in Pseudomonas aeruginosa biofilm formation by controlling the presence of the CdrA adhesin on the cell surface",
abstract = "Pseudomonas aeruginosa is a clinically relevant species involved in biofilm-based chronic infections. We provide evidence that the P. aeruginosa LapG protein functions as a periplasmic protease that can cleave the protein adhesin CdrA off the cell surface, and thereby plays a role in biofilm formation and biofilm dispersal. The P. aeruginosa LapG protein is shown to be a functional homolog of the Pseudomonas putida LapG protein which has previously been shown to function as a periplasmic protease that targets the surface adhesin LapA. Transposon mutagenesis and characterization of defined knockout mutants provided evidence that the CdrA adhesin is a target of LapG in P. aeruginosa. A wspF lapG double mutant was hyper-aggregating and hyper biofilm forming, whereas a wspF lapG cdrA triple mutant lost these phenotypes. In addition, western blot detection of CdrA in culture supernatants and whole-cell protein fractions showed that CdrA was retained in the whole-cell protein fraction when LapG was absent, whereas it was found in the culture supernatant when LapG was present. The finding that CdrA is a target of LapG in P. aeruginosa is surprising because CdrA has no homology to LapA.",
author = "Morten Rybtke and Jens Berthelsen and Liang Yang and Niels H{\o}iby and Michael Givskov and Tim Tolker-Nielsen",
note = "{\circledC} 2015 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.",
year = "2015",
month = "12",
doi = "10.1002/mbo3.301",
language = "English",
volume = "4",
pages = "917--30",
journal = "MicrobiologyOpen",
issn = "2045-8827",
publisher = "John Wiley and Sons Inc.",
number = "6",

}

RIS

TY - JOUR

T1 - The LapG protein plays a role in Pseudomonas aeruginosa biofilm formation by controlling the presence of the CdrA adhesin on the cell surface

AU - Rybtke, Morten

AU - Berthelsen, Jens

AU - Yang, Liang

AU - Høiby, Niels

AU - Givskov, Michael

AU - Tolker-Nielsen, Tim

N1 - © 2015 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.

PY - 2015/12

Y1 - 2015/12

N2 - Pseudomonas aeruginosa is a clinically relevant species involved in biofilm-based chronic infections. We provide evidence that the P. aeruginosa LapG protein functions as a periplasmic protease that can cleave the protein adhesin CdrA off the cell surface, and thereby plays a role in biofilm formation and biofilm dispersal. The P. aeruginosa LapG protein is shown to be a functional homolog of the Pseudomonas putida LapG protein which has previously been shown to function as a periplasmic protease that targets the surface adhesin LapA. Transposon mutagenesis and characterization of defined knockout mutants provided evidence that the CdrA adhesin is a target of LapG in P. aeruginosa. A wspF lapG double mutant was hyper-aggregating and hyper biofilm forming, whereas a wspF lapG cdrA triple mutant lost these phenotypes. In addition, western blot detection of CdrA in culture supernatants and whole-cell protein fractions showed that CdrA was retained in the whole-cell protein fraction when LapG was absent, whereas it was found in the culture supernatant when LapG was present. The finding that CdrA is a target of LapG in P. aeruginosa is surprising because CdrA has no homology to LapA.

AB - Pseudomonas aeruginosa is a clinically relevant species involved in biofilm-based chronic infections. We provide evidence that the P. aeruginosa LapG protein functions as a periplasmic protease that can cleave the protein adhesin CdrA off the cell surface, and thereby plays a role in biofilm formation and biofilm dispersal. The P. aeruginosa LapG protein is shown to be a functional homolog of the Pseudomonas putida LapG protein which has previously been shown to function as a periplasmic protease that targets the surface adhesin LapA. Transposon mutagenesis and characterization of defined knockout mutants provided evidence that the CdrA adhesin is a target of LapG in P. aeruginosa. A wspF lapG double mutant was hyper-aggregating and hyper biofilm forming, whereas a wspF lapG cdrA triple mutant lost these phenotypes. In addition, western blot detection of CdrA in culture supernatants and whole-cell protein fractions showed that CdrA was retained in the whole-cell protein fraction when LapG was absent, whereas it was found in the culture supernatant when LapG was present. The finding that CdrA is a target of LapG in P. aeruginosa is surprising because CdrA has no homology to LapA.

U2 - 10.1002/mbo3.301

DO - 10.1002/mbo3.301

M3 - Journal article

VL - 4

SP - 917

EP - 930

JO - MicrobiologyOpen

JF - MicrobiologyOpen

SN - 2045-8827

IS - 6

ER -

ID: 46284645