Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

SPD1590_iTRAQ - A Novel Iron Transporter SPD_1590 in Streptococcus pneumoniae Contributing to Bacterial Virulence Properties

ABSTRACT: Streptococcus pneumoniae has three main transporters for iron acquisition: PiaABC, PiuABC, and PitABC. Our previous study had shown that the mRNA and protein levels of SPD_1590 are significantly upregulated in a piuA/piaA/pitA triple mutant, suggesting that SPD_1590 might be a novel iron transporter in S. pneumoniae. In the present work, using spd1590-deleted and -overexpressing strains and the purified SPD_1590 protein, we show that SPD_1590 can bind hemin. 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.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Streptococcus Pneumoniae Serotype 2 (strain D39 / Nctc 7466)

TISSUE(S): Cell Culture

SUBMITTER: Xin Yu Miao

LAB HEAD: Xuesong Sun

PROVIDER: PXD008814 | Pride | 2018-08-08

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SPD1590_iTRAQ_1.raw	Raw
	SPD1590_iTRAQ_10.raw	Raw
	SPD1590_iTRAQ_11.raw	Raw
	SPD1590_iTRAQ_12.raw	Raw
	SPD1590_iTRAQ_13.raw	Raw

Items per page:

1 - 5 of 17

Publications

A Novel Iron Transporter SPD_1590 in Streptococcus pneumoniae Contributing to Bacterial Virulence Properties.

Miao Xinyu X He Jiaojiao J Zhang Liang L Zhao Xinlu X Ge Ruiguang R He Qing-Yu QY Sun Xuesong X

Frontiers in microbiology 20180720

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 -overexpressin ...[more]

PMID: 30079056

Similar Datasets

A Bifunctional SPD-0090 contributes virulence of Streptococcus pneumoniae by affecting iron transport and galactose metabolism

Project description:Streptococcus pneumoniae (S.pneumoniae) is a Gram-positive bacterial pathogen that colonizes on the mucosal surfaces of the host's nasopharynx and upper respiratory tract and results in pneumonia. In order to survive and infect the host, S.pneumoniae must have obtain essential nutrients, such as transition metal ions . Our previous study had shown that the mRNA and protein levels of SPD-0090 are significantly upregulated in the ΔpiuA/ΔpiaA/ΔpitA triple mutant (three major iron transports), but its detailed biological function is unknown. In this study, we found that the knockout spd-0090 gene induced a delayed growth in the medium with different sugar sources. F urther iTRAQ quantitative proteomics studies revealed that SPD-0090 affects galactose metabolism and iron ion transport system. Then RT-qPCR and intracellular galactose content assays showed that SPD-0090 affects galactose uptake, leads to reduced galactose utilization. In addition, in vitro biochemical assays showed that SPD-0090 is a hemin transporter and affects iron uptake. Notably the knockout of spd-0090 resulted in an enhanced infection ability of S.pneumonaie to Our study reveals that the dual function of SPD-0090 plays an important role in the virulence of S.pneumoniae.

2022-06-01 | PXD030183 | Pride

Transcriptional effect of various iron treatments on Caco-2 cells.

Project description:We investigated transcriptional response of CaCo-2 cells to iron treatments, we studied hemin effect by adding hemin to DMEM-FBS medium and iron deficiency effects in using an iron free medium compared to the same supplemented with FAC (ferric ammonium citrate). Keywords: various iron treatment, differential gene expression, hemin treatment, iron-free

2006-07-14 | GSE3573 | GEO

Transcription profiling of human CaCo-2 cells following various iron treatments

Project description:We investigated transcriptional response of CaCo-2 cells to iron treatments, we studied hemin effect by adding hemin to DMEM-FBS medium and iron deficiency effects in using an iron free medium compared to the same supplemented with FAC (ferric ammonium citrate). Experiment Overall Design: Biological replicates were used (3 samples) of each iron treatments (SF-FAC, SF-0, DMEM-FBS, DMEM-Hemin). Each sample was labelled with cy5 and a pool of each sample was constituted and labelled with cy3.

2008-01-19 | E-GEOD-3573 | biostudies-arrayexpress

How the presence of hemin affects the expression of all iron-uptake pathways in Pseudomonas aeruginosa cells

Project description:Iron is an essential nutriment for almost all organisms, but this metal is poorly bioavailable. During infection, bacteria access iron from the host by importing either iron or hemin. Pseudomonas aeruginosa, a Gram-negative pathogen, secretes two siderophores, pyoverdine (PVD) and pyochelin (PCH), to access iron and is also able to use many siderophores produced by other microorganisms (called xenosiderophores). To access hemin, P. aeruginosa uses three distinct uptake pathways, named Has, Phu, and Hxu. We previously showed that P. aeruginosa expresses the Has and Phu hemin uptake systems, as well as the PVD- and PCH-dependent iron-uptake pathways, in iron-restricted growth conditions using proteomic and RT-qPCR approaches. Here, using the same approach, we show that physiological concentrations of hemin in the bacterial growth medium result in the repression of the expression of the proteins of the PVD- and PCH-dependent iron-uptake pathways, leading to less production of these two siderophores. This indicates that the pathogen adapts its phenotype to use hemin as an iron source rather than produce PVD and PCH to access iron. Moreover, the presence of both hemin and a xenosiderophore resulted in (i) the strong induction of the expression of the proteins of the added xenosiderophore-uptake pathway, (ii) repression of the PVD- and PCH-dependent iron-uptake pathways, and (iii) no effect on the expression levels of the Has, Phu, or Hxu systems, indicating that bacteria use both xenosiderophores and hemin to access iron.

2022-03-15 | PXD028818 | Pride

Acetylome analysis of Streptococcus pneumoniae

Project description:Our dataset provides the first system-wide analysis of lysine acetylation in S. pneumoniae.

2018-01-29 | PXD007687 | Pride

Essential role of proline synthesis and the one-carbon metabolism pathways for systemic virulence of Streptococcus pneumoniae

Project description:Rapid adaptation to grow within the physiological conditions found in the host environment is an essential but poorly understood virulence requirement for systemic pathogens such as Streptococcus pneumoniae. We have now demonstrated an essential role for the one-carbon metabolism pathway and a conditional role depending on strain background for proline biosynthesis for S. pneumoniae growth in serum or CSF and therefore for systemic virulence. RNAseq data demonstrated that loss of one carbon metabolism or proline biosynthesis both have profound but differing effects on S. pneumoniae metabolism in human serum, identifying the metabolic processes dependent on each pathway during systemic infection. These data provide a more detailed understanding of the adaptations required by systemic bacterial pathogens in order to cause infection, and demonstrate that the requirement for some of these adaptations vary between strains from the same species and could therefore underpin strain variations in virulence potential.

2023-09-10 | E-MTAB-13289 | biostudies-arrayexpress

A Novel Iron Transporter SPD_1590 in Streptococcus pneumoniae Contributing to Bacterial Virulence Properties.

Project description: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 ?piuA/?piaA/?pitA 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.

| S-EPMC6062600 | biostudies-literature

Transcription profiling of human HeLa cells grown to subconfluent density and CaCo-2 cells grown to high density treated with an iron source (hemin) or an iron chelator (desferal)

Project description:HeLa cells grown to subconfluent density and CaCo-2 cells grown to high density were either treated with an iron source (hemin) or an iron chelator (desferal). Cells were harvested and RNA was prepared by RNA-Clean (Hybaid-AGS) and the RNA was subjected to a subsequent clean up using the RNeasy (Qiagen) clean up procedure.

2006-04-05 | E-MANP-1 | biostudies-arrayexpress

Proteomic study of a breast cancer cell line following hemin treatment

Project description:Heme, an iron-containing prosthetic group found in many proteins, carries out diverse biological functions such as electron transfer, oxygen storage and enzymatic reactions. Hemin, the oxidised form of heme, is used to treat porphyria and also to activate heme-oxygenase (HO) which catalyses the rate-limiting step in heme degradation. Our group has previously demonstrated that hemin displays antitumor activity in breast cancer (BC). The aim of this work has been to study the effect of hemin on protein expression modifications in a BC cell line to gain insight into the molecular mechanisms of hemin antitumor activity. For this purpose, we carried out proteome analysis by Mass Spectrometry (MS) which showed that 1309 proteins were significantly increased in hemin-treated cells, including HO-1 and the proteases that regulate HO-1 function, and 921 proteins were significantly decreased. Furthermore, the MS-data analysis showed that hemin regulates the expression of heme- and iron- related proteins, adhesion and cytoskeletal proteins, cancer signal transduction proteins and enzymes involved in lipid metabolism. By biochemical and cellular studies, we further corroborated the most relevant in-silico results. Altogether, these results show the multiple physiological effects that hemin treatment displays in BC and demonstrate its potential as anticancer agent.

2023-07-20 | PXD036701 | Pride

CodY of Streptococcus pneumoniae: link between nutritional gene regulation and virulence

Project description:CodY is a nutritional regulator mainly involved in amino acid metabolism. It has been extensively studied in Bacillis subtilis and Lactococcus lactis. We investigated the role of CodY in gene regulation and virulence of the human pathogen Streptococcus pneumoniae. We constructed a codY-mutant and examined the effect on gene and protein expression by microarray and 2D DIGE analysis. The pneumococcal CodY-regulon was found to consist predominantly of genes involved in amino acid metabolism, but also several other cellular processes, such as carbon metabolism and iron uptake. By means of electrophoretic mobility shift assays and DNA footprinting, we showed that most targets identified are under direct control of CodY. By mutating DNA predicted to represent the CodY-box based on the L. lactis consensus, we demonstrated that this sequence is indeed required for in vitro DNA-binding to target promoters. Similar to L. lactis, DNA-binding of CodY was enhanced in the presence of the branched chain amino acids isoleucine, leucine, and valine, and not by GTP. We observed in experimental mouse models that CodY is transcribed in the murine nasopharynx and lungs, and is specifically required for colonization. This finding was underscored by the diminished ability of the codY-mutant to adhere to nasopharyngeal cells in vitro. In conclusion, pneumococcal CodY predominantly regulates genes involved in amino acid metabolism and contributes to the early stages of infection, i.e. colonization of the nasopharynx. Keywords: codY CodY of Streptococcus pneumoniae: link between nutritional gene regulation and virulence

2010-05-25 | E-GEOD-7350 | biostudies-arrayexpress