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Published on: February 23, 2014
A Novel Iron Transporter SPD_1590 in Streptococcus pneumoniae Contributing to Bacterial Virulence Properties
Xinyu Miao1, Jiaojiao He1, Liang Zhang1
1Key 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.
Abstract:
Streptococcus pneumoniae, 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 ΔpiuA/ΔpiaA/ΔpitA triple mutant, suggesting that SPD_1590 might be a novel iron transporter in S. pneumoniae. In the present study, using spd1590-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.
Insights
Streptococcus pneumoniae utilizes SPD_1590, a novel iron transporter, to acquire essential iron, likely supplementing the PiuABC system. This transporter is crucial for bacterial virulence, enhancing our understanding of this pathogen.
Area of Science:
- Microbiology
- Molecular Biology
- Pathogen Research
Background:
- Streptococcus pneumoniae employs PiaABC, PiuABC, and PitABC for iron acquisition.
- Previous findings indicated SPD_1590 upregulation in iron transporter mutants.
Purpose of the Study:
- To investigate the role of SPD_1590 as a novel iron transporter in Streptococcus pneumoniae.
- To determine the contribution of SPD_1590 to bacterial virulence.
Main Methods:
- Construction and analysis of spd1590-knockout, -complemented, and -overexpressing strains.
- Purification and hemin-binding assays of SPD_1590 protein.
- iTRAQ quantitative proteomics and cell-infection studies.
Main Results:
- SPD_1590 directly binds hemin, suggesting a role in iron acquisition, potentially complementing PiuABC.
- SPD_1590 is essential for virulence properties of Streptococcus pneumoniae.
- Proteomics data revealed SPD_1590's involvement in metal-ion uptake pathways.
Conclusions:
- SPD_1590 is identified as a novel hemin-binding iron transporter in Streptococcus pneumoniae.
- SPD_1590 plays a significant role in the virulence of this important human pathogen.
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