Authors: Giltner, Carmen L.¹; van Schaik, Erin J.¹; Audette, Gerald F.¹; Kao, Dan²; Hodges, Robert S.²; Hassett, Daniel J.³; Irvin, Randall T.¹

Source: Molecular Microbiology, Volume 59, Number 4, February 2006 , pp. 1083-1096(14)

Publisher: Wiley-Blackwell

Abstract:

Summary

Pseudomonas aeruginosa readily binds to stainless steel and other abiotic surfaces, causing major problems in both the medical and food industries. In this study, we show that P. aeruginosa binds to abiotic surfaces in a concentration-dependent, saturable manner during the initial stages of biofilm formation. P. aeruginosa type IV pili mediate binding to stainless steel as a pilus-deficient strain does not bind to steel, purified type IV pili bound in a concentration-dependent, saturable manner, and purified pili competitively inhibited whole cell binding. PAK pili can also bind polystyrene and polyvinylchloride in a concentration-dependant and saturable manner. As an antibody specific for the C-terminal pilin receptor binding domain inhibited adherence to abiotic surfaces, the role of the C-terminal receptor binding domain in mediating binding to steel surfaces was examined. A synthetic peptide of the PAK pilin epithelial cell receptor binding domain [PAK(128–144)ox] bound directly to steel with high affinity. The interaction of pili with steel was specifically inhibited by this peptide with an apparent K_i of ∼0.2 nM and effectively inhibited the binding of viable homologous and heterologous P. aeruginosa strains to steel with an apparent K_i of ∼4 nM. A single point mutation (K130I) in the PAO receptor binding domain was observed to abolish binding to stainless steel while binding to human buccal epithelial cells was enhanced. Therefore, the C-terminal receptor binding domain appears to have evolved for binding a variety of surfaces.

Document Type: Research article

DOI: http://dx.doi.org/10.1111/j.1365-2958.2005.05002.x

Affiliations: 1: Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. 2: Department of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center at Fitzsimons, RC1 South Tower, Room 9121, PO Box 6511 MS 8101, Aurora, CO 80045, USA. 3: Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, Cincinnati, OH 45267-0524, USA.

Publication date: 2006-02-01

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