Literature DB >> 20048057

Influence of fatty acid precursors, including food preservatives, on the growth and fatty acid composition of Listeria monocytogenes at 37 and 10degreesC.

Mudcharee Julotok1, Atul K Singh, Craig Gatto, Brian J Wilkinson.   

Abstract

Listeria monocytogenes is a food-borne pathogen that grows at refrigeration temperatures and increases its content of anteiso-C(15:0) fatty acid, which is believed to be a homeoviscous adaptation to ensure membrane fluidity, at these temperatures. As a possible novel approach for control of the growth of the organism, the influences of various fatty acid precursors, including branched-chain amino acids and branched- and straight-chain carboxylic acids, some of which are also well-established food preservatives, on the growth and fatty acid composition of the organism at 37 degrees C and 10 degrees C were studied in order to investigate whether the organism could be made to synthesize fatty acids that would result in impaired growth at low temperatures. The results indicate that the fatty acid composition of L. monocytogenes could be modulated by the feeding of branched-chain amino acid, C(4), C(5), and C(6) branched-chain carboxylic acid, and C(3) and C(4) straight-chain carboxylic acid fatty acid precursors, but the growth-inhibitory effects of several preservatives were independent of effects on fatty acid composition, which were minor in the case of preservatives metabolized via acetyl coenzyme A. The ability of a precursor to modify fatty acid composition was probably a reflection of the substrate specificities of the first enzyme, FabH, in the condensation of primers of fatty acid biosynthesis with malonyl acyl carrier protein.

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Year:  2010        PMID: 20048057      PMCID: PMC2832362          DOI: 10.1128/AEM.01592-09

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  34 in total

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Journal:  Biochim Biophys Acta       Date:  2000-01-15

Review 2.  Membrane lipid homeostasis in bacteria.

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3.  Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases.

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4.  beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis.

Authors:  K H Choi; R J Heath; C O Rock
Journal:  J Bacteriol       Date:  2000-01       Impact factor: 3.490

5.  Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily.

Authors:  Dhirendra K Simanshu; H S Savithri; M R N Murthy
Journal:  J Mol Biol       Date:  2005-09-30       Impact factor: 5.469

6.  Cellular lipid fatty acid pattern heterogeneity between reference and recent food isolates of Listeria monocytogenes as a response to cold stress.

Authors:  Margarida Ribeiro Neunlist; Michel Federighi; Michel Laroche; Danièle Sohier; Gilles Delattre; Christine Jacquet; Nour-Eddine Chihib
Journal:  Antonie Van Leeuwenhoek       Date:  2005 Oct-Nov       Impact factor: 2.271

7.  Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases.

Authors:  K A Buss; D R Cooper; C Ingram-Smith; J G Ferry; D A Sanders; M S Hasson
Journal:  J Bacteriol       Date:  2001-01       Impact factor: 3.490

8.  Mechanism of synergistic inhibition of Listeria monocytogenes growth by lactic acid, monolaurin, and nisin.

Authors:  Oleksandr Tokarskyy; Douglas L Marshall
Journal:  Appl Environ Microbiol       Date:  2008-09-26       Impact factor: 4.792

9.  FabH selectivity for anteiso branched-chain fatty acid precursors in low-temperature adaptation in Listeria monocytogenes.

Authors:  Atul K Singh; Yong-Mei Zhang; Kun Zhu; Chitra Subramanian; Zhong Li; Radheshyam K Jayaswal; Craig Gatto; Charles O Rock; Brian J Wilkinson
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10.  Identification and characterization of a bacterial transport system for the uptake of pyruvate, propionate, and acetate in Corynebacterium glutamicum.

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  13 in total

1.  Branched-chain fatty acids promote Listeria monocytogenes intracellular infection and virulence.

Authors:  Yvonne Sun; Mary X D O'Riordan
Journal:  Infect Immun       Date:  2010-09-07       Impact factor: 3.441

2.  Fatty acids regulate stress resistance and virulence factor production for Listeria monocytogenes.

Authors:  Yvonne Sun; Brian J Wilkinson; Theodore J Standiford; Henry T Akinbi; Mary X D O'Riordan
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Review 3.  Regulation of bacterial pathogenesis by intestinal short-chain Fatty acids.

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Journal:  Adv Appl Microbiol       Date:  2013       Impact factor: 5.086

Review 4.  Gut Microbiota and Colonization Resistance against Bacterial Enteric Infection.

Authors:  Q R Ducarmon; R D Zwittink; B V H Hornung; W van Schaik; V B Young; E J Kuijper
Journal:  Microbiol Mol Biol Rev       Date:  2019-06-05       Impact factor: 11.056

5.  Utilization of multiple substrates by butyrate kinase from Listeria monocytogenes.

Authors:  Sirisha Sirobhushanam; Charitha Galva; Lauren P Saunders; Suranjana Sen; Radheshyam Jayaswal; Brian J Wilkinson; Craig Gatto
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6.  Short branched-chain C6 carboxylic acids result in increased growth, novel 'unnatural' fatty acids and increased membrane fluidity in a Listeria monocytogenes branched-chain fatty acid-deficient mutant.

Authors:  Suranjana Sen; Sirisha Sirobhushanam; Michael P Hantak; Peter Lawrence; J Thomas Brenna; Craig Gatto; Brian J Wilkinson
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7.  Broad substrate specificity of phosphotransbutyrylase from Listeria monocytogenes: A potential participant in an alternative pathway for provision of acyl CoA precursors for fatty acid biosynthesis.

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8.  The role of two branched-chain amino acid transporters in Staphylococcus aureus growth, membrane fatty acid composition and virulence.

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9.  Growth and membrane fluidity of food-borne pathogen Listeria monocytogenes in the presence of weak acid preservatives and hydrochloric acid.

Authors:  Ioannis Diakogiannis; Anita Berberi; Eleni Siapi; Angeliki Arkoudi-Vafea; Lydia Giannopoulou; Sofia K Mastronicolis
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10.  Structural and functional characterisation of TesA - a novel lysophospholipase A from Pseudomonas aeruginosa.

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