PslD is a secreted protein required for biofilm formation by Pseudomonas aeruginosa.

Standard

PslD is a secreted protein required for biofilm formation by Pseudomonas aeruginosa. / Campisano, Andrea; Schröder, Christine; Schemionek, Mirle; Overhage, Joerg; Rehm, Bernd H A.

In: APPL ENVIRON MICROB, Vol. 72, No. 4, 4, 2006, p. 3066-3068.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Campisano, A, Schröder, C, Schemionek, M, Overhage, J & Rehm, BHA 2006, 'PslD is a secreted protein required for biofilm formation by Pseudomonas aeruginosa.', APPL ENVIRON MICROB, vol. 72, no. 4, 4, pp. 3066-3068. <http://www.ncbi.nlm.nih.gov/pubmed/16598021?dopt=Citation>

APA

Campisano, A., Schröder, C., Schemionek, M., Overhage, J., & Rehm, B. H. A. (2006). PslD is a secreted protein required for biofilm formation by Pseudomonas aeruginosa. APPL ENVIRON MICROB, 72(4), 3066-3068. [4]. http://www.ncbi.nlm.nih.gov/pubmed/16598021?dopt=Citation

Vancouver

Campisano A, Schröder C, Schemionek M, Overhage J, Rehm BHA. PslD is a secreted protein required for biofilm formation by Pseudomonas aeruginosa. APPL ENVIRON MICROB. 2006;72(4):3066-3068. 4.

Bibtex

@article{edede3af63414e3abbac1efcd5bea4a3,
title = "PslD is a secreted protein required for biofilm formation by Pseudomonas aeruginosa.",
abstract = "The function of pslD, which is part of the psl operon from Pseudomonas aeruginosa, was investigated in this study. The psl operon is involved in exopolysaccharide biosynthesis and biofilm formation. An isogenic marker-free pslD deletion mutant of P. aeruginosa PAO1 which was deficient in the formation of differentiated biofilms was generated. Expression of only the pslD gene coding region restored the wild-type phenotype. A C-terminal, hexahistidine tag fusion enabled the identification of PslD. LacZ and PhoA translational fusions with PslD indicated that PslD is a secreted protein required for biofilm formation, presumably via its role in exopolysaccharide export.",
author = "Andrea Campisano and Christine Schr{\"o}der and Mirle Schemionek and Joerg Overhage and Rehm, {Bernd H A}",
year = "2006",
language = "Deutsch",
volume = "72",
pages = "3066--3068",
journal = "APPL ENVIRON MICROB",
issn = "0099-2240",
publisher = "American Society for Microbiology",
number = "4",

}

RIS

TY - JOUR

T1 - PslD is a secreted protein required for biofilm formation by Pseudomonas aeruginosa.

AU - Campisano, Andrea

AU - Schröder, Christine

AU - Schemionek, Mirle

AU - Overhage, Joerg

AU - Rehm, Bernd H A

PY - 2006

Y1 - 2006

N2 - The function of pslD, which is part of the psl operon from Pseudomonas aeruginosa, was investigated in this study. The psl operon is involved in exopolysaccharide biosynthesis and biofilm formation. An isogenic marker-free pslD deletion mutant of P. aeruginosa PAO1 which was deficient in the formation of differentiated biofilms was generated. Expression of only the pslD gene coding region restored the wild-type phenotype. A C-terminal, hexahistidine tag fusion enabled the identification of PslD. LacZ and PhoA translational fusions with PslD indicated that PslD is a secreted protein required for biofilm formation, presumably via its role in exopolysaccharide export.

AB - The function of pslD, which is part of the psl operon from Pseudomonas aeruginosa, was investigated in this study. The psl operon is involved in exopolysaccharide biosynthesis and biofilm formation. An isogenic marker-free pslD deletion mutant of P. aeruginosa PAO1 which was deficient in the formation of differentiated biofilms was generated. Expression of only the pslD gene coding region restored the wild-type phenotype. A C-terminal, hexahistidine tag fusion enabled the identification of PslD. LacZ and PhoA translational fusions with PslD indicated that PslD is a secreted protein required for biofilm formation, presumably via its role in exopolysaccharide export.

M3 - SCORING: Zeitschriftenaufsatz

VL - 72

SP - 3066

EP - 3068

JO - APPL ENVIRON MICROB

JF - APPL ENVIRON MICROB

SN - 0099-2240

IS - 4

M1 - 4

ER -