Laminin-binding epitope on gp43 from Paracoccidioides brasiliensis is recognized by a monoclonal antibody raised against Staphylococcus aureus laminin receptor

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorVicentini, A. P.
dc.creatorMoraes, J. Z.
dc.creatorGesztesi, J. L.
dc.creatorFranco, M. F.
dc.creatorDe Souza, W.
dc.creatorLopes, J. D.
dc.date2014-05-27T11:18:13Z
dc.date2016-10-25T18:14:23Z
dc.date2014-05-27T11:18:13Z
dc.date2016-10-25T18:14:23Z
dc.date1997-03-03
dc.date.accessioned2017-04-06T00:49:21Z
dc.date.available2017-04-06T00:49:21Z
dc.identifierJournal of Medical and Veterinary Mycology, v. 35, n. 1, p. 37-43, 1997.
dc.identifier0268-1218
dc.identifierhttp://hdl.handle.net/11449/65071
dc.identifierhttp://acervodigital.unesp.br/handle/11449/65071
dc.identifier10.1080/02681219780000851
dc.identifierWOS:A1997WJ67100007
dc.identifier2-s2.0-0031045220
dc.identifier2-s2.0-79961242524
dc.identifierhttp://dx.doi.org/10.1080/02681219780000851
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/886829
dc.descriptionAdhesion is regarded as an important step in the pathogenesis of several microorganisms. Thus, the ability to recognize extracellular matrix proteins, such as laminin or fibronectin, has been correlated with invasiveness. Studying the already characterized laminin-binding protein of Paracoccidioides brasiliensis, the 43 kDa glycoprotein (gp43), we evaluated whether MAb 1.H12, raised against the laminin-binding protein from Staphylococcus aureus, cross-reacts with that fungal protein. By immunoblot analysis we show that MAb 1.H12 recognizes gp43. This interaction is able to inhibit the laminin-mediated adhesion to epithelial cells as well as the P. brasiliensis infection in vivo. Moreover, through immunoenzymatic assays, we show that MAb 1.H12 recognizes gp43 in solid phase and that this interaction is partially inhibited by the addition of anti-gp43 MAbs. These results show that MAb 1.H12 recognizes the gp43, suggesting the presence of an epitope similar to those found in the other laminin-binding proteins from phylogenetically very distant cells. These findings reinforce the possibility of evolutionary conservation of such epitopes.
dc.languageeng
dc.relationJournal of Medical and Veterinary Mycology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectanti-S. aureus
dc.subjectLaminin-binding
dc.subjectMab 1.H12
dc.subjectP. brasiliensis
dc.subjectepitope
dc.subjectglycoprotein
dc.subjectlaminin
dc.subjectlaminin binding protein
dc.subjectlaminin receptor
dc.subjectmonoclonal antibody
dc.subjectadhesion
dc.subjectcell invasion
dc.subjectcontrolled study
dc.subjectevolution
dc.subjectextracellular matrix
dc.subjectnonhuman
dc.subjectparacoccidioides brasiliensis
dc.subjectphylogeny
dc.subjectstaphylococcus aureus
dc.subjectAnimals
dc.subjectAntibodies, Monoclonal
dc.subjectBinding Sites
dc.subjectCell Adhesion
dc.subjectCell Line
dc.subjectCricetinae
dc.subjectDogs
dc.subjectEpithelium
dc.subjectEpitopes
dc.subjectExtracellular Matrix Proteins
dc.subjectGranuloma
dc.subjectHumans
dc.subjectKidney
dc.subjectLaminin
dc.subjectLung Neoplasms
dc.subjectMale
dc.subjectMicroscopy, Electron, Scanning
dc.subjectParacoccidioides
dc.subjectReceptors, Laminin
dc.subjectStaphylococcus aureus
dc.subjectTestis
dc.subjectParacoccidioides brasiliensis
dc.titleLaminin-binding epitope on gp43 from Paracoccidioides brasiliensis is recognized by a monoclonal antibody raised against Staphylococcus aureus laminin receptor
dc.typeOtro


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