Identification Of New Sphingomyelinases D In Pathogenic Fungi And Other Pathogenic Organisms

dc.creatorDias-Lopes C.
dc.creatorNeshich I.A.P.
dc.creatorNeshich G.
dc.creatorOrtega J.M.
dc.creatorGranier C.
dc.creatorChavez-Olortegui C.
dc.creatorMolina F.
dc.creatorFelicori L.
dc.date2013
dc.date2015-06-25T19:10:17Z
dc.date2015-11-26T15:07:56Z
dc.date2015-06-25T19:10:17Z
dc.date2015-11-26T15:07:56Z
dc.date.accessioned2018-03-28T22:18:23Z
dc.date.available2018-03-28T22:18:23Z
dc.identifier
dc.identifierPlos One. , v. 8, n. 11, p. - , 2013.
dc.identifier19326203
dc.identifier10.1371/journal.pone.0079240
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84891380008&partnerID=40&md5=c934cb7e86143ef91920e9fc94a119df
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/88483
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/88483
dc.identifier2-s2.0-84891380008
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1257577
dc.descriptionSphingomyelinases D (SMases D) or dermonecrotic toxins are well characterized in Loxosceles spider venoms and have been described in some strains of pathogenic microorganisms, such as Corynebacterium sp. After spider bites, the SMase D molecules cause skin necrosis and occasional severe systemic manifestations, such as acute renal failure. In this paper, we identified new SMase D amino acid sequences from various organisms belonging to 24 distinct genera, of which, 19 are new. These SMases D share a conserved active site and a C-terminal motif. We suggest that the C-terminal tail is responsible for stabilizing the entire internal structure of the SMase D Tim barrel and that it can be considered an SMase D hallmark in combination with the amino acid residues from the active site. Most of these enzyme sequences were discovered from fungi and the SMase D activity was experimentally confirmed in the fungus Aspergillus flavus. Because most of these novel SMases D are from organisms that are endowed with pathogenic properties similar to those evoked by these enzymes alone, they might be associated with their pathogenic mechanisms. © 2013 Dias-Lopes et al.
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dc.languageen
dc.publisher
dc.relationPLoS ONE
dc.rightsaberto
dc.sourceScopus
dc.titleIdentification Of New Sphingomyelinases D In Pathogenic Fungi And Other Pathogenic Organisms
dc.typeArtículos de revistas


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