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The regulation of antimicrobial peptide resistance in the transition to insect symbiosis
Author(s) -
Clayton Adam L.,
Enomoto Shinichiro,
Su Yinghua,
Dale Colin
Publication year - 2017
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13598
Subject(s) - biology , response regulator , regulator , bacteria , antimicrobial , two component regulatory system , antimicrobial peptides , peptide , gene , microbiology and biotechnology , insect , kinase , host (biology) , biochemistry , genetics , bacterial protein , botany , mutant
Summary 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 Mg 2+ , Ca 2+ , 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 Mg 2+ , Ca 2+ 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.