Crotacetin, a novel snake venom C-type lectin homolog of convulxin, exhibits an unpredictable antimicrobial activity

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dc.contributor.authorRadis-Baptista, G.
dc.contributor.authorMoreno, FBMB
dc.contributor.authorNogueira, L. D.
dc.contributor.authorMartins, AMC
dc.contributor.authorToyama, D. D.
dc.contributor.authorToyama, M. H.
dc.contributor.authorCavada, B. S.
dc.contributor.authorde Azevedo, W. F.
dc.contributor.authorYamane, T.
dc.contributor.institutionUniversidade Federal do Ceará (UFC)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionInstituto de Pesquisas Energéticas e Nucleares (IPEN)
dc.contributor.institutionCBA
dc.date.accessioned2014-05-20T14:02:23Z
dc.date.available2014-05-20T14:02:23Z
dc.date.issued2006-01-01
dc.description.abstractSnake venom (sv) C-type lectins encompass a group of hemorrhagic toxins that are capable of interfering with blood stasis. A very well-studied svC-type lectin is the heterodimeric toxin, convulxin (CVX), from the venom of South American rattlesnake Crotalus durissus terrificus. CVX is able to activate platelets and induce their aggregation by acting via p62/GPVI collagen receptor. By using polymerase chain reaction homology screening, we have cloned several cDNA precursors of CVX subunit homologs. One of them, named crotacetin (CTC) beta-subunit, predicts a polypeptide with a topology very similar to the tridimensional conformations of other subunits of CVX-like snake toxins, as determined by computational analysis. Using gel permeation and reverse-phase high-performance liquid chromatography, CTC was purified from C. durissus venoms. CTC can be isolated from the venom of several C. durissus subspecies, but its quantitative predominance is in the venom of C. durissus cascavella. Functional analysis indicates that CTC induces platelet aggregation, and, importantly, exhibits an antimicrobial activity against Gram-positive and -negative bacteria, comparable with CVX.en
dc.description.affiliationFed Univ Ceara, Dept Biochem & Mol Biol, Ceara, Brazil
dc.description.affiliationFed Univ Ceara, Dept Clin & Toxicol Anal, Ceara, Brazil
dc.description.affiliationUNESP, Dept Phys, IBILCE, São Paulo, Brazil
dc.description.affiliationUniv Estadual Campinas, Dept Biochem, São Paulo, Brazil
dc.description.affiliationUNESP, Dept Fundamental Chem, São Paulo, Brazil
dc.description.affiliationIPEN, CNEN, Mol Biol Lab, São Paulo, Brazil
dc.description.affiliationCBA, Manaus, Amazonas, Brazil
dc.description.affiliationUnespUNESP, Dept Phys, IBILCE, São Paulo, Brazil
dc.description.affiliationUnespUNESP, Dept Fundamental Chem, São Paulo, Brazil
dc.format.extent412-423
dc.identifierhttp://dx.doi.org/10.1385/CBB:44:3:412
dc.identifier.citationCell Biochemistry and Biophysics. Totowa: Humana Press Inc., v. 44, n. 3, p. 412-423, 2006.
dc.identifier.doi10.1385/CBB:44:3:412
dc.identifier.issn1085-9195
dc.identifier.urihttp://hdl.handle.net/11449/21993
dc.identifier.wosWOS:000237403800011
dc.language.isoeng
dc.publisherHumana Press Inc
dc.relation.ispartofCell Biochemistry and Biophysics
dc.relation.ispartofjcr1.455
dc.relation.ispartofsjr0,581
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectCrotalus durisssus venompt
dc.subjectsnake venom C-type lectinpt
dc.subjectcrotacetinpt
dc.subjectconvulxinpt
dc.subjectplatelet aggregationpt
dc.subjectantimicrobial activitypt
dc.titleCrotacetin, a novel snake venom C-type lectin homolog of convulxin, exhibits an unpredictable antimicrobial activityen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights
dcterms.rightsHolderHumana Press Inc
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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