McClelland Erin E, Ramagopal Udupi A, Rivera Johanna, Cox James, Nakouzi Antonio, Prabu Moses M, Almo Steven C, Casadevall Arturo
Department of Biology, Middle Tennessee State University, Murfreesboro, Tennessee, United States of America.
Department of Biochemistry and Department of Physiology & Biophysics, Albert Einstein College of Medicine, Bronx, New York, United States of America.
PLoS Pathog. 2016 Sep 1;12(9):e1005849. doi: 10.1371/journal.ppat.1005849. eCollection 2016 Sep.
The pathogenic yeast Cryptococcus neoformans causes cryptococcosis, a life-threatening fungal disease. C. neoformans has multiple virulence mechanisms that are non-host specific, induce damage and interfere with immune clearance. Microarray analysis of C. neoformans strains serially passaged in mice associated a small gene (CNAG_02591) with virulence. This gene, hereafter identified as HVA1 (hypervirulence-associated protein 1), encodes a protein that has homologs of unknown function in plant and animal fungi, consistent with a conserved mechanism. Expression of HVA1 was negatively correlated with virulence and was reduced in vitro and in vivo in both mouse- and Galleria-passaged strains of C. neoformans. Phenotypic analysis in hva1Δ and hva1Δ+HVA1 strains revealed no significant differences in established virulence factors. Mice infected intravenously with the hva1Δ strain had higher fungal burden in the spleen and brain, but lower fungal burden in the lungs, and died faster than mice infected with H99W or the hva1Δ+HVA1 strain. Metabolomics analysis demonstrated a general increase in all amino acids measured in the disrupted strain and a block in the TCA cycle at isocitrate dehydrogenase, possibly due to alterations in the nicotinamide cofactor pool. Macrophage fungal burden experiments recapitulated the mouse hypervirulent phenotype of the hva1Δ strain only in the presence of exogenous NADPH. The crystal structure of the Hva1 protein was solved, and a comparison of structurally similar proteins correlated with the metabolomics data and potential interactions with NADPH. We report a new gene that modulates virulence through a mechanism associated with changes in fungal metabolism.
致病性酵母新型隐球菌可引发隐球菌病,这是一种危及生命的真菌疾病。新型隐球菌具有多种毒力机制,这些机制是非宿主特异性的,会造成损害并干扰免疫清除。对在小鼠体内连续传代的新型隐球菌菌株进行微阵列分析,发现一个小基因(CNAG_02591)与毒力相关。该基因,此后被鉴定为HVA1(高毒力相关蛋白1),编码一种在动植物真菌中具有未知功能同源物的蛋白质,这与一种保守机制相符。HVA1的表达与毒力呈负相关,在新型隐球菌的小鼠传代菌株和蜡螟传代菌株中,其在体外和体内的表达均降低。对hva1Δ和hva1Δ+HVA1菌株的表型分析显示,既定的毒力因子没有显著差异。静脉注射hva1Δ菌株的小鼠在脾脏和大脑中的真菌负荷较高,但在肺部的真菌负荷较低,并且比感染H99W或hva1Δ+HVA1菌株的小鼠死亡更快。代谢组学分析表明,在 disrupted 菌株中测得的所有氨基酸普遍增加,并且在异柠檬酸脱氢酶处三羧酸循环受阻,这可能是由于烟酰胺辅因子池的改变所致。巨噬细胞真菌负荷实验仅在外源NADPH存在的情况下才重现了hva1Δ菌株的小鼠高毒力表型。解析了Hva1蛋白的晶体结构,对结构相似蛋白的比较与代谢组学数据以及与NADPH的潜在相互作用相关。我们报告了一个通过与真菌代谢变化相关的机制调节毒力的新基因。