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A glycine betaine importer limits Salmonella stress resistance and tissue colonization by reducing trehalose production
Author(s) -
Pilonieta M. Carolina,
Nagy Toni A.,
Jorgensen Dana R.,
Detweiler Corrella S.
Publication year - 2012
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/j.1365-2958.2012.08022.x
Subject(s) - trehalose , betaine , biology , salmonella enterica , osmoprotectant , salmonella , microbiology and biotechnology , bacteria , mutant , biochemistry , glycine , wild type , proline , gene , amino acid , genetics
Summary Mechanisms by which Salmonella establish chronic infections are not well understood. Microbes respond to stress by importing or producing compatible solutes, small molecules that stabilize proteins and lipids. The Salmonella locus opuABCD (also called OpuC) encodes a predicted importer of the compatible solute glycine betaine. Under stress conditions, if glycine betaine cannot be imported, Salmonella enterica produce the disaccharide trehalose, a highly effective compatible solute. We demonstrate that strains lacking opuABCD accumulate more trehalose under stress conditions than wild‐type strains. ΔopuABCD mutant strains are more resistant to high‐salt, low‐pH and ‐hydrogen peroxide, conditions that mimic aspects of innate immunity, in a trehalose‐dependent manner. In addition, Δ opuABCD mutant strains require the trehalose production genes to out‐compete wild‐type strains in mice and macrophages. These data suggest that in the absence of opuABCD , trehalose accumulation increases bacterial resistance to stress in broth and mice. Thus, opuABCD reduces bacterial colonization via a mechanism that limits trehalose production. Mechanisms by which microbes limit disease may reveal novel pathways as therapeutic targets.