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Pseudechis australis Venomics: Adaptation for a Defense against Microbial Pathogens and Recruitment of Body Transferrin

dc.contributor.authorGeorgieva, Dessislava
dc.contributor.authorSeifert, Jana
dc.contributor.authorOehler, Michaela
dc.contributor.authorvon Bergen, Martin
dc.contributor.authorSpencer, Patrick
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.authorGenov, Nicolay
dc.contributor.authorBetzel, Christian
dc.contributor.institutionUniv Hamburg
dc.contributor.institutionUFZ Helmholtz Ctr Environm Res
dc.contributor.institutionInstituto de Pesquisas Energéticas e Nucleares (IPEN)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionBulgarian Acad Sci
dc.date.accessioned2014-05-20T14:02:31Z
dc.date.available2014-05-20T14:02:31Z
dc.date.issued2011-05-01
dc.description.abstractThe venom composition of Pseudechis australis, a widely distributed in Australia reptile, was analyzed by 2-DE and mass spectrometric analysis. In total, 102 protein spots were identified as venom toxins. The gel is dominated by horizontal trains of spots with identical or very similar molecular masses but differing in the pI values. This suggests possible post-translational modifications of toxins, changing their electrostatic charge. The results demonstrate a highly specialized biosynthesis of toxins destroying the hemostasis (P-III metalloproteases, SVMPs), antimicrobial proteins (L-amino acid oxidases, LAAOs, and transferrin-like proteins, TFLPs), and myotoxins (phospholipase A(2)s, PLA(2)s). The three transferrin isoforms of the Australian P. avstralis (Elapidae snake) venom are highly homologous to the body transferrin of the African Lamprophis fuliginosus (Colubridae), an indication for the recruitment of body transferrin. The venomic composition suggests an adaptation for a defense against microbial pathogens from the prey. Transferrins have not previously been reported as components of elapid or other snake venoms. Ecto-5'-nucleotidases (5'-NTDs), nerve growth factors (VNGFs), and a serine proteinase inhibitor (SPI) were also identified. The venom composition and enzymatic activities explain the clinical manifestation of the king brown snakebite. The results can be used for medical, scientific, and biotechnological purposes.en
dc.description.affiliationUniv Hamburg, Inst Biochem & Mol Biol, Lab Struct Biol Infect & Inflammat, DESY, D-22603 Hamburg, Germany
dc.description.affiliationUFZ Helmholtz Ctr Environm Res, Dept Prote, D-04318 Leipzig, Germany
dc.description.affiliationIPEN CNEN SP, Ctr Biotecnol, BR-05508000 São Paulo, Brazil
dc.description.affiliationIBILCE UNESP, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationBulgarian Acad Sci, Inst Organ Chem, BU-1113 Sofia, Bulgaria
dc.description.affiliationUnespIBILCE UNESP, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdDFG: BE 1443-18-1
dc.description.sponsorshipIdDFG: BE1443
dc.format.extent2440-2464
dc.identifierhttp://dx.doi.org/10.1021/pr101248e
dc.identifier.citationJournal of Proteome Research. Washington: Amer Chemical Soc, v. 10, n. 5, p. 2440-2464, 2011.
dc.identifier.doi10.1021/pr101248e
dc.identifier.issn1535-3893
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/22038
dc.identifier.wosWOS:000290234800027
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal of Proteome Research
dc.relation.ispartofjcr3.950
dc.relation.ispartofsjr1,818
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectSnake venomicen
dc.subjectPseudechis australisen
dc.subject2-D electrophoresisen
dc.subjectelectrospray mass spectrometryen
dc.subjectvenom transferrinen
dc.subjectEnzymatic activityen
dc.titlePseudechis australis Venomics: Adaptation for a Defense against Microbial Pathogens and Recruitment of Body Transferrinen
dc.typeArtigo
dcterms.licensehttp://pubs.acs.org/page/copyright/journals/faqs.html
dcterms.rightsHolderAmer Chemical Soc
dspace.entity.typePublication
unesp.author.lattes9162508978945887[6]
unesp.author.orcid0000-0003-2460-1145[6]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentFísica - IBILCEpt

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