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The regulation of antimicrobial peptide resistance in the transition to insect symbiosis.
Clayton, Adam L; Enomoto, Shinichiro; Su, Yinghua; Dale, Colin.
Afiliación
  • Clayton AL; Department of Biology, University of Utah, Salt Lake City, UT, USA.
  • Enomoto S; Department of Biology, University of Utah, Salt Lake City, UT, USA.
  • Su Y; Department of Biology, University of Utah, Salt Lake City, UT, USA.
  • Dale C; Department of Biology, University of Utah, Salt Lake City, UT, USA.
Mol Microbiol ; 103(6): 958-972, 2017 03.
Article en En | MEDLINE | ID: mdl-27987256
ABSTRACT
Many bacteria utilize two-component systems consisting of a sensor kinase and a transcriptional response regulator to detect environmental signals and modulate gene expression for adaptation. The response regulator PhoP and its cognate sensor kinase PhoQ compose a two-component system known for its role in responding to low levels of Mg2+ , Ca2+ , pH and to the presence of antimicrobial peptides and activating the expression of genes involved in adaptation to host association. Compared with their free-living relatives, mutualistic insect symbiotic bacteria inhabit a static environment where the requirement for sensory functions is expected to be relaxed. The insect symbiont, Sodalis glossinidius, requires PhoP to resist killing by host derived antimicrobial peptides. However, the S. glossinidius PhoQ was found to be insensitive to Mg2+ , Ca2+ and pH. Here they show that Sodalis praecaptivus, a close non host-associated relative of S. glossinidius, utilizes a magnesium sensing PhoP-PhoQ and an uncharacterized MarR-like transcriptional regulator (Sant_4061) to control antimicrobial peptide resistance in vitro. While the inactivation of phoP, phoQ or Sant_4061 completely retards the growth of S. praecaptivus in the presence of an antimicrobial peptide in vitro, inactivation of both phoP and Sant_4061 is necessary to abrogate growth of this bacterium in an insect host.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Péptidos Catiónicos Antimicrobianos / Gorgojos / Enterobacteriaceae Límite: Animals Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Péptidos Catiónicos Antimicrobianos / Gorgojos / Enterobacteriaceae Límite: Animals Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos