Exocellular proteolytic activity of Paracoccidioides brasiliensis: cleavage of components associated with the basement membrane

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dc.contributor.authorPuccia, R.
dc.contributor.authorCarmona, A. K.
dc.contributor.authorGesztesi, J. L.
dc.contributor.authorJuliano, L.
dc.contributor.authorTravassos, L. R.
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T12:30:41Z
dc.date.available2016-01-24T12:30:41Z
dc.date.issued1998-10-01
dc.description.abstractWe have previously characterized an exocellular serine-thiol proteinase activity in Paracoccidioides brasiliensis, using as substrates peptides analogous of the internally quenched fluorogenic peptide Abz-MKWLTL-EDDnp. in this communication, detection of maximal proteinase activity in the culture supernatant fluids followed the abrupt increase in the medium pH, owing to the accumulation of ammonia generated by urease activity. Culture supernatant fluids collected at the peak of proteinase activity against Abz-MRKLTL-EDDnp were able to cleave components of the basal membrane of the extracellular matrix (EM), including laminin, fibronectin, collagen type IV and proteoglycans, and the proteolytic activity was selectively inhibited both by PMSF and p-HMB (sodium 7-hydroxymercuribenzoate), which are also specific inhibitors of the serine-thiol proteinase. Human collagen I, bovine fibrinogen, human immunoglobulin G, BSA or P. brasiliensis gp43 were resistant to proteolysis. the kinetics of appearance of the proteinase activity against EM substrates coincided with that of proteolysis of Abz-MKRLTL-EDDnp. Moreover, chromatographic fractions of culture supernatants containing the serine-thiol proteinase at high specific activity were also active against EM substrates. These data suggest the involvement of this enzyme activity in the degradation of the basement membrane, which is the first step for fungal tissue invasion.en
dc.description.affiliationUniversidade Federal de São Paulo, Disciplina Biol Celular, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Disciplina Biol Celular, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, BR-04023062 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent345-348
dc.identifierhttp://dx.doi.org/10.1080/02681219880000541
dc.identifier.citationMedical Mycology. Oxford: Blackwell Science Ltd, v. 36, n. 5, p. 345-348, 1998.
dc.identifier.doi10.1080/02681219880000541
dc.identifier.issn1369-3786
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/25968
dc.identifier.wosWOS:000076537800015
dc.language.isoeng
dc.publisherBlackwell Science Ltd
dc.relation.ispartofMedical Mycology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectbasement membraneen
dc.subjectexocellular proteinaseen
dc.subjectParacoccidioides brasiliensisen
dc.titleExocellular proteolytic activity of Paracoccidioides brasiliensis: cleavage of components associated with the basement membraneen
dc.typeinfo:eu-repo/semantics/article
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