Document Detail

Investigation of the <i>Listeria monocytogenes</i> Scott A acid tolerance response and associated physiological and phenotypic features via whole proteome analysis.
MedLine Citation:
PMID:  22372944     Owner:  NLM     Status:  Publisher    
The global proteomic responses of the foodborne pathogen <i>Listeria monocytogenes</i> strain Scott A, during active growth and transition to stationary growth phase under progressively more acidic conditions, created by addition of lactic acid and HCl, was investigated using label-free liquid chromatography/tandem mass spectrometry. Approximately 56% of the Scott A proteome was quantitatively assessable and the data provides insight into its acquired acid tolerance response (ATR) as well as the relation of ATR to growth phase transition. Alterations in protein abundance due to acid stress were focussed in proteins belonging to the <i>L. monocytogenes</i> common genome, with few strain-dependent proteins involved. However, one of the two complete prophage genomes appeared to enter lysogeny. During progressive acidification growth rate and yield were reduced 55% and 98%, respectively, in comparison to non-acidified control cultures. The maintenance of growth rate was determined to be connected to activation of cytoplasmic pH homeostatic mechanisms while cellular reproductive-related and cell component turnover proteins were markedly more abundant in acid stressed cultures. Cell biomass accumulation was impeded predominantly due to repression of phosphodonor-linked enzymes involved with sugar phosphotransfer, glycolysis, and cell wall polymer biosynthesis. Acidification caused a shift from heterofermentation to an oxidatively stressed state in which ATP appears to be generated mainly through the pyruvate dehydrogenase/pyruvate oxidase/phosphotransacetylase/acetate kinase and branched chain acid dehydrogenase pathways. Analysis of regulons indicated energy conservation occurs due to repression by the GTP/isoleucine sensor CodY and also the RelA mediated stringent response. Whole proteome analysis proved to be an effective way to highlight proteins involved with the acquisition of the ATR.
John P Bowman; Esta Hages; Rolf E Nilsson; Chawalit Kocharunchitt; Tom Ross
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-2-29
Journal Detail:
Title:  Journal of proteome research     Volume:  -     ISSN:  1535-3907     ISO Abbreviation:  -     Publication Date:  2012 Feb 
Date Detail:
Created Date:  2012-2-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101128775     Medline TA:  J Proteome Res     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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