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http://purl.uniprot.org/citations/25343965http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25343965http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25343965http://www.w3.org/2000/01/rdf-schema#comment"

Background

The second messenger cyclic diguanylate (c-di-GMP) plays a central role in bacterial adaptation to extracellular stimuli, controlling processes such as motility, biofilm development, cell development and, in some pathogens, virulence. The intracellular level of c-di-GMP is controlled by the complementary activities of diguanylate cyclases containing a GGDEF domain and two classes of c-di-GMP phosphodiesterases containing an EAL or HD-GYP hydrolytic domain. Compared to the GGDEF and EAL domains, the functions of HD-GYP domain family proteins are poorly characterized. The human diarrheal pathogen Vibrio cholerae encodes nine putative HD-GYP domain proteins. To determine the contributions of HD-GYP domain proteins to c-di-GMP signaling in V. cholerae, we systematically analyzed the enzymatic functionality of each protein and their involvement in processes known to be regulated by c-di-GMP: motility, biofilm development and virulence.

Results

Complementary in vitro and in vivo experiments showed that four HD-GYP domain proteins are active c-di-GMP phosphodiesterases: VC1295, VC1348, VCA0210 and VCA0681. Mutation of individual HD-GYP domain genes, as well as combinatorial mutations of multiple HD-GYP domain genes, had no effect on motility or biofilm formation of V. cholerae under the conditions tested. Furthermore, no single HD-GYP domain gene affected intestinal colonization by V. cholerae in an infant mouse model. However, inactivation of multiple HD-GYP domain genes, including the four encoding functional phosphodiesterases, significantly attenuated colonization.

Conclusions

These results indicate that the HD-GYP family of c-di-GMP phosphodiesterases impacts signaling by this second messenger during infection. Altogether, this work greatly furthers the understanding of this important family of c-di-GMP metabolic enzymes and demonstrates a role for HD-GYP domain proteins in the virulence of V. cholerae."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.org/dc/terms/identifier"doi:10.1186/s12866-014-0272-9"xsd:string
http://purl.uniprot.org/citations/25343965http://purl.org/dc/terms/identifier"doi:10.1186/s12866-014-0272-9"xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"Kariisa A."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"Kariisa A."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"McKee R.W."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"McKee R.W."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"Mudrak B."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"Mudrak B."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"Tamayo R."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"Tamayo R."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"Whitaker C."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/author"Whitaker C."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/name"BMC Microbiol."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/name"BMC Microbiol."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/pages"272"xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/pages"272"xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/title"A systematic analysis of the in vitro and in vivo functions of the HD-GYP domain proteins of Vibrio cholerae."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/title"A systematic analysis of the in vitro and in vivo functions of the HD-GYP domain proteins of Vibrio cholerae."xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/25343965http://purl.uniprot.org/core/volume"14"xsd:string
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