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Besnoitia besnoiti protein disulfide isomerase (BbPDI): molecular characterization, expression and in silico modelling

2011-10Journal article Open access
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dc.contributor.authorMarcelino, Eduardo
dc.contributor.authorMartins, Tiago M.
dc.contributor.authorMorais, Joana B.
dc.contributor.authorNolasco, Sofia
dc.contributor.authorCortes, Helder
dc.contributor.authorHemphill, Andrew
dc.contributor.authorLeitão, Alexandre
dc.contributor.authorNovo, Carlos
dc.date.accessioned2014-01-02T14:41:09Z
dc.date.available2014-01-02T14:41:09Z
dc.date.issued2011-10
dc.description.abstractBesnoitia besnoiti is an apicomplexan parasite responsible for bovine besnoitiosis, a disease with a high prevalence in tropical and subtropical regions and re-emerging in Europe. Despite the great economical losses associated with besnoitiosis, this disease has been underestimated and poorly studied, and neither an effective therapy nor an efficacious vaccine is available. Protein disulfide isomerase (PDI) is an essential enzyme for the acquisition of the correct three-dimensional structure of proteins. Current evidence suggests that in Neosporacaninum and Toxoplasmagondii, which are closely related to B. besnoiti, PDI play an important role in host cell invasion, is a relevant target for the host immune response, and represents a promising drug target and/or vaccine candidate. In this work, we present the nucleotide sequence of the B. besnoiti PDI gene. BbPDI belongs to the thioredoxin-like superfamily (cluster 00388) and is included in the PDI_a family (cluster defined cd02961) and the PDI_a_PDI_a'_c subfamily (cd02995). A 3D theoretical model was built by comparative homology using Swiss-Model server, using as a template the crystallographic deduced model of Tapasin-ERp57 (PDB code 3F8U chain C). Analysis of the phylogenetic tree for PDI within the phylum apicomplexa reinforces the close relationship among B. besnoiti, N. caninum and T. gondii. When subjected to a PDI-assay based on the polymerisation of reduced insulin, recombinant BbPDI expressed in E. coli exhibited enzymatic activity, which was inhibited by bacitracin. Antiserum directed against recombinant BbPDI reacted with PDI in Western blots and by immunofluorescence with B. besnoiti tachyzoites and bradyzoites.por
dc.identifier.citationMarcelino E, Martins TM, Morais JB, Nolasco S, Cortes H, Hemphill A, et al. Besnoitia besnoiti protein disulfide isomerase (BbPDI): molecular characterization, expression and in silico modelling. Exp Parasitol. 2011;129(2):164-74.por
dc.identifier.issn1090-2449
dc.identifier.urihttp://hdl.handle.net/10400.21/3047
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.relation.publisherversionhttp://www.sciencedirect.com/science/article/pii/S0014489411001998#por
dc.subjectAmino acid sequencepor
dc.subjectAntibody specificitypor
dc.subjectBacitracinpor
dc.subjectBase sequencepor
dc.subjectBlotting, Westernpor
dc.subjectCattlepor
dc.subjectCercopithecus aethiopspor
dc.subjectCloning, Molecularpor
dc.subjectComputer simulationpor
dc.subjectDNA, Protozoanpor
dc.subjectGene expression regulationpor
dc.subjectGenome, Protozoanpor
dc.subjectImaging, Three-dimensionalpor
dc.subjectModels, Molecularpor
dc.subjectMolecular sequence datapor
dc.subjectPhylogenypor
dc.subjectProtein conformationpor
dc.subjectProtein disulfide-isomerasespor
dc.subjectSarcocystidaepor
dc.subjectSequence analysis, DNApor
dc.titleBesnoitia besnoiti protein disulfide isomerase (BbPDI): molecular characterization, expression and in silico modellingpor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage174por
oaire.citation.startPage164por
oaire.citation.titleExperimental Parasitologypor
oaire.citation.volume129por
rcaap.rightsopenAccesspor
rcaap.typearticlepor

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