Miao Xinyu, He Jiaojiao, Zhang Liang, Zhao Xinlu, Ge Ruiguang, He Qing-Yu, Sun Xuesong
Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University, Guangzhou, China.
Key Laboratory of Gene Engineering of the Ministry of Education, State Key Laboratory of Biocontrol, College of Life Sciences, Sun Yat-sen University, Guangzhou, China.
Front Microbiol. 2018 Jul 20;9:1624. doi: 10.3389/fmicb.2018.01624. eCollection 2018.
, a Gram-positive human pathogen, has evolved three main transporters for iron acquisition from the host: PiaABC, PiuABC, and PitABC. Our previous study had shown that the mRNA and protein levels of SPD_1590 are significantly upregulated in the Δ/Δ/Δ triple mutant, suggesting that SPD_1590 might be a novel iron transporter in . In the present study, using -knockout, -complemented, and -overexpressing strains and the purified SPD_1590 protein, we show that SPD_1590 can bind hemin, probably supplementing the function of PiuABC, to provide the iron necessary for the bacterium. Furthermore, the results of iTRAQ quantitative proteomics and cell-infection studies demonstrate that, similarly to other metal-ion uptake proteins, SPD_1590 is important for bacterial virulence properties. Overall, these results provide a better understanding of the biology of this clinically important bacterium.
作为一种革兰氏阳性人类病原体,已经进化出三种主要的从宿主获取铁的转运蛋白:PiaABC、PiuABC和PitABC。我们之前的研究表明,在Δ/Δ/Δ三重突变体中,SPD_1590的mRNA和蛋白质水平显著上调,这表明SPD_1590可能是该病原体中的一种新型铁转运蛋白。在本研究中,使用基因敲除、基因互补和基因过表达菌株以及纯化的SPD_1590蛋白,我们表明SPD_1590可以结合血红素,可能补充PiuABC的功能,为细菌提供所需的铁。此外,iTRAQ定量蛋白质组学和细胞感染研究结果表明,与其他金属离子摄取蛋白类似,SPD_1590对细菌的毒力特性很重要。总体而言,这些结果有助于更好地理解这种临床重要细菌的生物学特性。