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2017-11-24Zeitschriftenartikel DOI: 10.1038/s41598-017-12796-4
Disulfide loop cleavage of Legionella pneumophila PlaA boosts lysophospholipase A activity
dc.contributor.authorLang, Christina
dc.contributor.authorHiller, Miriam
dc.contributor.authorFlieger, Antje
dc.date.accessioned2018-05-07T20:59:09Z
dc.date.available2018-05-07T20:59:09Z
dc.date.created2018-01-30
dc.date.issued2017-11-24none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/rexBlGu6r0FNA/PDF/24qFZbprQt7E2.pdf
dc.identifier.urihttp://edoc.rki.de/176904/2951
dc.description.abstractL. pneumophila, an important facultative intracellular bacterium, infects the human lung and environmental protozoa. At least fifteen phospholipases A (PLA) are encoded in its genome. Three of which, namely PlaA, PlaC, and PlaD, belong to the GDSL lipase family abundant in bacteria and higher plants. PlaA is a lysophospholipase A (LPLA) that destabilizes the phagosomal membrane in absence of a protective factor. PlaC shows PLA and glycerophospholipid: cholesterol acyltransferase (GCAT) activities which are activated by zinc metalloproteinase ProA via cleavage of a disulphide loop. In this work, we compared GDSL enzyme activities, their secretion, and activation of PlaA. We found that PlaA majorly contributed to LPLA, PlaC to PLA, and both substrate-dependently to GCAT activity. Western blotting revealed that PlaA and PlaC are type II-secreted and both processed by ProA. Interestingly, ProA steeply increased LPLA but diminished GCAT activity of PlaA. Deletion of 20 amino acids within a predicted disulfide loop of PlaA had the same effect. In summary, we propose a model by which ProA processes PlaA via disulfide loop cleavage leading to a steep increase in LPLA activity. Our results help to further characterize the L. pneumophila GDSL hydrolases, particularly PlaA, an enzyme acting in the Legionella-containing phagosome.eng
dc.language.isoeng
dc.publisherRobert Koch-Institut, Infektionskrankheiten / Erreger
dc.subject.ddc610 Medizin
dc.titleDisulfide loop cleavage of Legionella pneumophila PlaA boosts lysophospholipase A activity
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-10057089
dc.identifier.doi10.1038/s41598-017-12796-4
dc.identifier.doihttp://dx.doi.org/10.25646/2876
local.edoc.container-titleScientific Reports
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttps://www.nature.com/articles/s41598-017-12796-4
local.edoc.container-publisher-nameNature Publishing Group
local.edoc.container-volume7
local.edoc.container-year2017

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