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Article Dans Une Revue Protein Science Année : 2012

Sensing the messenger: The diverse ways that bacteria signal through c-di-GMP

Résumé

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.
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Dates et versions

hal-03117469 , version 1 (21-01-2021)

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Petya V. Krasteva, Krista Michelle Giglio, Holger Sondermann. Sensing the messenger: The diverse ways that bacteria signal through c-di-GMP. Protein Science, 2012, 21, pp.929 - 948. ⟨10.1002/pro.2093⟩. ⟨hal-03117469⟩

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