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

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

Author Puccia, R. Google Scholar
Carmona, A. K. Google Scholar
Gesztesi, J. L. Google Scholar
Juliano, L. Google Scholar
Travassos, L. R. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Abstract We 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.
Keywords basement membrane
exocellular proteinase
Paracoccidioides brasiliensis
Language English
Date 1998-10-01
Published in Medical Mycology. Oxford: Blackwell Science Ltd, v. 36, n. 5, p. 345-348, 1998.
ISSN 1369-3786 (Sherpa/Romeo, impact factor)
Publisher Blackwell Science Ltd
Extent 345-348
Origin http://dx.doi.org/10.1080/02681219880000541
Access rights Closed access
Type Article
Web of Science ID WOS:000076537800015
URI http://repositorio.unifesp.br/handle/11600/25968

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