Liquid medium for growth of Legionella pneumophila

Ristroph, Joseph D.; Hedlund, Kenneth; Allen, Richard B.

doi:10.1128/jcm.11.1.19-21.1980

Cited by 121 publications

(53 citation statements)

References 5 publications

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“…). As mentioned above, L. pneumophila exhibits a putative serine transport protein (Lpp2269) to take up serine from the medium , and serine is an important carbon and energy source for L. pneumophila during growth in medium . It was also mentioned that cell‐free extracts of L. pneumophila exhibit high serine dehydratase activity .…”

Section: Metabolic Features Of L Pneumophila In Vitromentioning

confidence: 99%

“…Early (radiotracer) experiments revealed that amino acids serve as the main carbon and energy source of L. pneumophila when growing in vitro in different media . From these experiments, Ser, Thr, Glu and Tyr were identified as preferred substrates in vitro , and Cys, Gln, Ser, Met, Val, Glu, Tyr, Thr and Arg were shown to support growth in vivo .…”

Section: Metabolic Features Of L Pneumophila In Vitromentioning

confidence: 99%

“…Various experimental studies and the analysis of various genome sequences revealed that L. pneumophila is auxotrophic for Arg, Cys, Ile, Leu, Met, Thr and Val, and the amino acids Arg, Cys, Ile, Leu, Met, (Phe), Ser, Thr, (Tyr) and Val are essential for growth . Cysteine is absolutely required for the growth of legionellae, and media must be supplemented with cysteine to support growth of L. pneumophila , but this is not true for L. oakridgensis , a less virulent Legionella species .…”

Section: Metabolic Features Of L Pneumophila In Vitromentioning

confidence: 99%

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The life stage‐specific pathometabolism of Legionella pneumophila

Eisenreich

Heuner

2016

FEBS Letters

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The genus Legionella belongs to Gram-negative bacteria found ubiquitously in aquatic habitats, where it grows in natural biofilms and replicates intracellularly in various protozoa (amoebae, ciliates). L. pneumophila is known as the causative agent of Legionnaires' disease, since it is also able to replicate in human alveolar macrophages, finally leading to inflammation of the lung and pneumonia. To withstand the degradation by its host cells, a Legionellacontaining vacuole (LCV) is established for intracellular replication, and numerous effector proteins are secreted into the host cytosol using a type four B secretion system (T4BSS). During intracellular replication, Legionella has a biphasic developmental cycle that alternates between a replicative and a transmissive form. New knowledge about the host-adapted and life stagedependent metabolism of intracellular L. pneumophila revealed a bipartite metabolic network with life stage-specific usages of amino acids (e.g. serine), carbohydrates (e.g. glucose) and glycerol as major substrates. These metabolic features are associated with the differentiation of the intracellular bacteria, and thus have an important impact on the virulence of L. pneumophila.

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Section: Metabolic Features Of L Pneumophila In Vitromentioning

confidence: 99%

Section: Metabolic Features Of L Pneumophila In Vitromentioning

confidence: 99%

Section: Metabolic Features Of L Pneumophila In Vitromentioning

confidence: 99%

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The life stage‐specific pathometabolism of Legionella pneumophila

Eisenreich

Heuner

2016

FEBS Letters

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“…pUC18 [8] was used as a vector for plasmid construction and pGEM-T (Promega) as a PCR product cloning vector. E. coli was grown on/in LB medium at 37³C with or without 1.5% agar [9] and L. pneumophila was grown in BCYE agar (Difco) plates or YEB [10] at 35³C.…”

Section: Bacterial Strains Plasmid and Growth Conditionsmentioning

confidence: 99%

Identification of a novel periplasmic catalase-peroxidase KatA of Legionella pneumophila

Amemura-Maekawa¹

1999

FEMS Microbiology Letters

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A gene katA that encodes a novel catalase-peroxidase was cloned from the chromosome of Legionella pneumophila. The nucleotide sequence revealed that KatA was highly homologous to members of the bacterial bifunctional catalase-peroxidase family. In addition, KatA has a N-terminal signal sequence and was considered to be present in the periplasm of the bacterium. ß 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. PII: S 0 3 7 8 -1 0 9 7 ( 9 9 ) 0 0 2 5 4 -2

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“…Growth and radiolabeling. Kinetics of growth were determined by inoculating organisms into 20 ml of yeast extract broth (YEB [26]; 10 g of yeast extract, 0.4 g of L-cysteine hydrochloride, 0.25 g of ferric pyrophosphate [pH 6.9]) and the optical density at 660 nm (OD6w) was monitored at hourly intervals. To minimize accumulation of superoxide radicals, which are reported to have a toxic effect oh growing cells (15), the following steps were taken: (i) culture medium was sterilized by filtration through a 0.2-,um Millipore filter instead of by autoclaving, (ii) cysteine was added just before inoculation, and (iii) the media were protected from light during bacterial growth.…”

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confidence: 99%

Identification of protein antigens of Legionella pneumophila serogroup 1

Pearlman¹,

Engleberg²,

Eisenstein³

1985

Infect Immun

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Growth of Legionella pneumophila serogroup 1 in yeast extract broth was standardized, and protein profiles of detergent-solubilized cells were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Over 30 protein bands were identified, 6 of which were more prominent both in Coomassie brilliant blue-stained profiles and in fluorograms with intrinsically radiolabeled bacteria. These major proteins were 22,000 dalton (22K), 24K, 43K, 63K, 76K, and 78K. We found that the 24K and 63K major proteins were antigenic, as demonstrated both by radioimmunoprecipitation (RIP) of [35S]methionine-labeled organisms and by immunoblotting with rabbit hyperimmune sera. In addition, both techniques detected antigens migrating at 58K, 72K, 76K, and 78K. The major 22K and 43K major proteins and antigens migrating at 25.5K, 29K, and 46K were only detected by radioimmunoprecipitation, whereas antigens of 19K, 48K, 53K, and 68K were detected only by immunoblotting. Cell-surface localization of the proteins was determined by a modified radioimmunoprecipitation assay designed to react specifically with surface antigens and by the use of hyperimmune sera that had been extepsively preabsorbed with intact cells to deplete the sgra of antibodies directed against surface components. The 22K, 24K, 43K, 63K, and 78K major proteins and several minor proteins were found to be located on the surface of L. pneumophila cells.

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Liquid medium for growth of Legionella pneumophila

Cited by 121 publications

References 5 publications

The life stage‐specific pathometabolism of Legionella pneumophila

The life stage‐specific pathometabolism of Legionella pneumophila

Identification of a novel periplasmic catalase-peroxidase KatA of Legionella pneumophila

Identification of protein antigens of Legionella pneumophila serogroup 1

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