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Med Mycol ; 41(4): 309-20, 2003 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-12964724

RESUMO

Cryptococcus neoformans secretes 3-hydroxyanthranilate (3HAA), but the utility is unknown. Exogenous 3HAA promoted growth of cultures starved for iron with transferrin, presumably by releasing Fe(III) reductively. Exogenous 3HAA protected C. neoformans from strong oxidants, suggesting a role in resistance to killing by immune cells. 3HAA represents an endogenous laccase substrate, in that crude laccase preparations convert 3HAA to cinnabarinic acid, whereas 3HAA concentrations are higher in Lac- mutants. We isolated hypersecreting mutants as highly fluorescent clones. Because C. neoformans has been isolated from rotting wood, we looked for a role in degradation of lignin. Using cyclic voltammetry, we found no electrochemical evidence that organic oxidation products of 3HAA are capable of oxidizing lignin. We found neither cellulose dehydrogenase nor lignin peroxidase enzymic activity, nor did C. neoformans grow on cellulose as carbon source. We found no evidence for production of Fenton reagent by cultures, even in the presence of transition metal ions or of those and 3HAA. The biological utility of 3HAA may be related to its functions as reducing agent and, conceivably, as laccase substrate. It does not appear to attack wood, nor does C. neoformans appear to have a mechanism to rot wood.


Assuntos
Ácido 3-Hidroxiantranílico/metabolismo , Cryptococcus neoformans/metabolismo , Substâncias Redutoras/metabolismo , Madeira , Antioxidantes/metabolismo , Biodegradação Ambiental , Desidrogenases de Carboidrato/metabolismo , Cryptococcus neoformans/genética , Cryptococcus neoformans/crescimento & desenvolvimento , Ferro/metabolismo , Lacase , Lignina/metabolismo , Estresse Oxidativo , Oxirredutases/metabolismo , Peroxidases/metabolismo , Transferrina/metabolismo
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