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首页> 外文期刊>Medical mycology: official publication of the International Society for Human and Animal Mycology >The copper, zinc superoxide dismutase gene of Penicillium marneffei: cloning, characterization, and differential expression during phase transition and macrophage infection.
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The copper, zinc superoxide dismutase gene of Penicillium marneffei: cloning, characterization, and differential expression during phase transition and macrophage infection.

机译:马尔尼菲青霉的铜,锌超氧化物歧化酶基因:在相变和巨噬细胞感染期间的克隆,鉴定和差异表达。

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摘要

Superoxide dismutase (SOD) is an enzyme that converts superoxide radicals into hydrogen peroxide and oxygen molecules. SOD has been shown to contribute to the virulence of many human-pathogenic fungi through its ability to neutralize toxic levels of reactive oxygen species generated by the host. SOD has also been speculated to be important in the pathogenesis of fungal infections, but the role of this enzyme has not been rigorously investigated. In this report, we isolated and characterized the copper, zinc superoxide dismutase gene, designated sodA, from the important human pathogenic fungus, Penicillium marneffei. The putative SodA polypeptide consisted of 154 amino acids and exhibited a significant level of similarity to other fungal Cu, Zn SODs. Differential expression of the sodA gene in P. marneffei was demonstrated by semi-quantitative RT-PCR. Apparently, the sodA transcript accumulated in conidia, but expression was downregulated in the mycelia phase. In contrast, transcript expression was upregulated in the yeast phase as well as during macrophage infection. The significantly higher expression of the sodA transcript during macrophage infection suggests that this gene might play an important role in stress responses and in the adaptation of P. marneffei to the internal macrophage environment. The latter may serve as a putative virulence factor of this fungus allowing for survival in the host cell.
机译:超氧化物歧化酶(SOD)是一种将超氧化物自由基转化为过氧化氢和氧分子的酶。 SOD具有中和宿主产生的活性氧的毒性水平的能力,已被证明对许多人致病性真菌具有致病性。还已推测SOD在真菌感染的发病机理中很重要,但尚未对该酶的作用进行严格的研究。在本报告中,我们从重要的人类致病真菌马尔尼菲青霉中分离并鉴定了铜,锌超氧化物歧化酶基因,称为sodA。推定的SodA多肽由154个氨基酸组成,与其他真菌Cu,Zn SOD表现出显着的相似性。通过半定量RT-PCR证实了sodA基因在马尔尼菲假单胞菌中的差异表达。显然,sodA转录物在分生孢子中积累,但在菌丝体期表达被下调。相反,在酵母期以及巨噬细胞感染期间,转录物表达被上调。在巨噬细胞感染期间,sodA转录物的表达明显较高,表明该基因可能在应激反应和马尔内菲疟原虫对内部巨噬细胞环境的适应中起重要作用。后者可作为该真菌的假定毒力因子,使其在宿主细胞中存活。

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