Bacterial cyclic AMP-phosphodiesterase activity coordinates biofilm formation

Biofilm-related infections are a major contributor to human disease, and the capacity for surface attachment and biofilm formation are key attributes for the pathogenesis of microbes. Serratia marcescens type I fimbriae-dependent biofilms are coordinated by the adenylate cyclase, CyaA, and the cycli...

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Published in:PloS one 2013-07, Vol.8 (7), p.e71267-e71267
Main Authors: Kalivoda, Eric J, Brothers, Kimberly M, Stella, Nicholas A, Schmitt, Matthew J, Shanks, Robert M Q
Format: Article
Language:English
Subjects:
Adenosine monophosphate
Adenylate cyclase
Bacteria
Bacteria - genetics
Bacteria - growth & development
Bacteria - metabolism
Biofilms
Biology
Cell division
Cyclic AMP
Cyclic AMP - metabolism
Defects
E coli
Escherichia coli
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Fimbriae, Bacterial - metabolism
Fimbriae, Bacterial - ultrastructure
Gene expression
Gene Expression Regulation, Bacterial
Gene Order
Genome, Bacterial
Homeostasis
Hydrolysis
In vivo methods and tests
Laboratories
Molecular Sequence Data
Motility
Mutation
Pathogenesis
Phosphodiesterase
Pili
Plasmids
Proteins
Pseudomonas aeruginosa
Receptors, Cyclic AMP - metabolism
RNA polymerase
Salmonella
Salmonella Typhimurium
Serratia marcescens - genetics
Serratia marcescens - growth & development
Serratia marcescens - metabolism
Vibrio cholerae
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description Biofilm-related infections are a major contributor to human disease, and the capacity for surface attachment and biofilm formation are key attributes for the pathogenesis of microbes. Serratia marcescens type I fimbriae-dependent biofilms are coordinated by the adenylate cyclase, CyaA, and the cyclic 3',5'-adenosine monophosphate (cAMP)-cAMP receptor protein (CRP) complex. This study uses S. marcescens as a model system to test the role of cAMP-phosphodiesterase activity in controlling biofilm formation. Herein we describe the characterization of a putative S. marcescens cAMP-phosphodiesterase gene (SMA3506), designated as cpdS, and demonstrated to be a functional cAMP-phosphodiesterase both in vitro and in vivo. Deletion of cpdS resulted in defective biofilm formation and reduced type I fimbriae production, whereas multicopy expression of cpdS conferred a type I fimbriae-dependent hyper-biofilm. Together, these results support a model in which bacterial cAMP-phosphodiesterase activity modulates biofilm formation.
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Serratia marcescens type I fimbriae-dependent biofilms are coordinated by the adenylate cyclase, CyaA, and the cyclic 3',5'-adenosine monophosphate (cAMP)-cAMP receptor protein (CRP) complex. This study uses S. marcescens as a model system to test the role of cAMP-phosphodiesterase activity in controlling biofilm formation. Herein we describe the characterization of a putative S. marcescens cAMP-phosphodiesterase gene (SMA3506), designated as cpdS, and demonstrated to be a functional cAMP-phosphodiesterase both in vitro and in vivo. Deletion of cpdS resulted in defective biofilm formation and reduced type I fimbriae production, whereas multicopy expression of cpdS conferred a type I fimbriae-dependent hyper-biofilm. 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subjects Adenosine monophosphate
Adenylate cyclase
Bacteria
Bacteria - genetics
Bacteria - growth & development
Bacteria - metabolism
Biofilms
Biology
Cell division
Cyclic AMP
Cyclic AMP - metabolism
Defects
E coli
Escherichia coli
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Fimbriae, Bacterial - metabolism
Fimbriae, Bacterial - ultrastructure
Gene expression
Gene Expression Regulation, Bacterial
Gene Order
Genome, Bacterial
Homeostasis
Hydrolysis
In vivo methods and tests
Laboratories
Molecular Sequence Data
Motility
Mutation
Pathogenesis
Phosphodiesterase
Pili
Plasmids
Proteins
Pseudomonas aeruginosa
Receptors, Cyclic AMP - metabolism
RNA polymerase
Salmonella
Salmonella Typhimurium
Serratia marcescens - genetics
Serratia marcescens - growth & development
Serratia marcescens - metabolism
Vibrio cholerae
title Bacterial cyclic AMP-phosphodiesterase activity coordinates biofilm formation
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