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Sensing the messenger: The diverse ways that bacteria signal through c‐di‐GMP
Author(s) -
Krasteva Petya Violinova,
Giglio Krista Michelle,
Sondermann Holger
Publication year - 2012
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2093
Subject(s) - second messenger system , intracellular , signal transduction , biofilm , biology , receptor , virulence , bacteria , function (biology) , phosphodiesterase , microbiology and biotechnology , computational biology , enzyme , biochemistry , genetics , gene
An intracellular second messenger unique to bacteria, c‐di‐GMP, has gained appreciation as a key player in adaptation and virulence strategies, such as biofilm formation, persistence, and cytotoxicity. Diguanylate cyclases containing GGDEF domains and phosphodiesterases containing either EAL or HD‐GYP domains have been identified as the enzymes controlling intracellular c‐di‐GMP levels, yet little is known regarding signal transmission and the sensory targets for this signaling molecule. Although limited in number, identified c‐di‐GMP receptors in bacteria are characterized by prominent diversity and multilevel impact. In addition, c‐di‐GMP has been shown to have immunomodulatory effects in mammals and several eukaryotic c‐di‐GMP sensors have been proposed. The structural biology of c‐di‐GMP receptors is a rapidly developing field of research, which holds promise for the development of novel therapeutics against bacterial infections. In this review, we highlight recent advances in identifying bacterial and eukaryotic c‐di‐GMP signaling mechanisms and emphasize the need for mechanistic structure–function studies on confirmed signaling targets.