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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Proteins and Peptidases from Conidia and Mycelia of Scedosporium apiospermum Strain HLPB

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Author(s):
Pereira, Martha Machado [1] ; Silva, Bianca Alcantara [1] ; Pinto, Marcia Ribeiro [2] ; Barreto-Bergter, Eliana [1] ; Souza dos Santos, Andre Luis [1]
Total Authors: 5
Affiliation:
[1] Univ Fed Rio de Janeiro, Dept Microbiol Geral, IMPPG, CCS, Ilha Fundao, BR-21941902 Rio De Janeiro - Brazil
[2] Univ Sao Paulo, Inst Ciencias Biol, Dept Microbiol, Sao Paulo - Brazil
Total Affiliations: 2
Document type: Journal article
Source: Mycopathologia; v. 167, n. 1, p. 25-30, JAN 2009.
Web of Science Citations: 16
Abstract

The conidia-mycelia transformation is an essential step during the life cycle of the fungal human pathogens of the Pseudallescheria boydii complex. In the present study, we have analyzed the protein and peptidase profiles in two distinct morphological stages, conidia and mycelia, of Scedosporium apiospermum sensu stricto. Proteins synthesized by the mycelia, migrating at the ranges of 62-48 and 22-18 kDa, were not detected from the conidial extract. Conidia produced a single cellular peptidase of 28 kDa able to digest copolymerized albumin, while mycelia yielded 6 distinct peptidases ranging from 90 to 28 kDa. All proteolytic enzymes were active at acidic pH and fully inhibited by 1,10-phenanthroline, characterizing these activities as metallo-type peptidases. Quantitative peptidase assay, using soluble albumin, showed a high metallopeptidase production in mycelial cells in comparison with conidia. The regulated expression of proteins and peptidases in different morphological stages of S. apiospermum represents a potential target for isolation of stage-specific markers for biochemical and immunological analysis. (AU)