dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributorClinica de Alergologia de Pouso Alegre
dc.date.accessioned2014-05-20T13:55:29Z
dc.date.available2014-05-20T13:55:29Z
dc.date.created2014-05-20T13:55:29Z
dc.date.issued2012-09-01
dc.identifierJournal of Proteome Research. Washington: Amer Chemical Soc, v. 11, n. 9, p. 4643-4653, 2012.
dc.identifier1535-3893
dc.identifierhttp://hdl.handle.net/11449/19855
dc.identifier10.1021/pr300451g
dc.identifierWOS:000308389900022
dc.identifier2901888624506535
dc.description.abstractFire ants are well-known by their aggressive stinging behavior, causing many stinging incidents of medical importance. The limited availability of fire ant venom for scientific and clinical uses has restricted, up to now, the knowledge about the biochemistry, immunology, and pharmacology of these venoms. For this study, S. invicta venom was obtained commercially and used for proteomic characterization. For this purpose, the combination of gel-based and gel-free proteomic strategies was used to assign the proteomic profile of the venom from the fire ant S. invicta. This experimental approach permitted the identification of 46 proteins, which were organized into four different groups according to their potential role in fire ant venom: true venom components, housekeeping proteins, body muscle proteins, and proteins involved in chemical communication. The active venom components that may not present toxic roles were classified into three subgroups according to their potential functions: self-venom protection, colony asepsis, and chemical communication. Meanwhile, the proteins classified as true toxins, based on their functions after being injected into the victims' bodies by the fire ants, were classified in five other subgroups: proteins influencing the homeostasis of the victims, neurotoxins, proteins that promote venom diffusion, proteins that cause tissue damage/inflammation, and allergens.
dc.languageeng
dc.publisherAmer Chemical Soc
dc.relationJournal of Proteome Research
dc.relation3.950
dc.relation1,818
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectHymenoptera
dc.subjectallergen
dc.subjecttoxin
dc.subjectproteomic analysis
dc.subjectmass spectrometry
dc.subjectshotgun proteomics
dc.subjectenvenoming mechanism
dc.titleProteomic View of the Venom from the Fire Ant Solenopsis invicta Buren
dc.typeArtículos de revistas


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