AdcAII, A New Pneumococcal Zn-Binding Protein Homologous with ABC Transporters: Biochemical and Structural Analysis

Loisel, Elodie; Jacquamet, Lilian; Serre, Laurence; Bauvois, Cédric; Ferrer, J.L.; Vernet, Thierry; Guilmi, Anne Marie Di; Durmort, Claire

doi:10.1016/j.jmb.2008.05.068

Cited by 108 publications

(149 citation statements)

References 57 publications

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“…Instead, promoters, but no transcription terminators, were identified for lmb and yfnA, two genes located upstream of phtD, which tended to indicate that those genes are organized in an operon system. This corroborates the recent finding that phtD may be expressed in a large operon system together with the four genes upstream (Loisel et al, 2008). Nevertheless, the fact that a promoter was identified for yfnA and for lmb indicates that transcription may start at these locations, meaning that phtD-containing transcripts of different length may be produced.…”

Section: Discussionsupporting

confidence: 90%

“…Nevertheless, the fact that a promoter was identified for yfnA and for lmb indicates that transcription may start at these locations, meaning that phtD-containing transcripts of different length may be produced. In addition, an adcR binding site was identified upstream of the lmb gene (Loisel et al, 2008;Panina et al, 2003), suggesting that a zinc-regulated bicistronic transcript with lmb and phtD may also exist. In line with this, Spellerberg et al (1999) showed that the group B streptococcal lmb gene is co-transcribed with a gene whose product shows 67 % sequence similarity to the first 225 (phtE) and first 228 (phtA, phtD and phtB) amino acids of pht gene products (accession no.…”

Section: Discussionmentioning

confidence: 99%

“…1). This gene product was also recently denoted as AdcAII, and described as an ABC transporter-like zinc-binding protein (Loisel et al, 2008). A 1392 bp ORF, located 142 bp upstream of the lmb gene homologue, codes for a protein showing 64 % sequence similarity to the Bacillus subtilis metabolite transporter YfnA protein (accession no.…”

Section: Characterization Of the Pht Genesmentioning

confidence: 99%

“…More specifically, some studies highlighted a link between the Pht family and zinc. Indeed, AdcR-binding sites have been found in the upstream regions of the pht genes (Loisel et al, 2008), AdcR being described as a transcription factor that regulates zinc uptake (Panina et al, 2003). Furthermore, the crystal structure of a portion of PhtA revealed the presence of zinc ions bound to a histidine triad domain (RiboldiTunnicliffe et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…4(a) (lanes 1-3), the regions yfnA to phtD were amplified by RT-PCR. Moreover, Loisel et al (2008) have demonstrated that this phtD transcript also encodes, in addition to yfnA, lmb and phtD, the two genes upstream of yfnA (ccdA, which is involved in the biogenesis of cytochrome c, and spr0904, which shows similarity to thioredoxine). Interestingly, the identification of a putative promoter upstream of the lmb gene (Fig.…”

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confidence: 99%

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Transcriptional regulation, occurrence and putative role of the Pht family of Streptococcus pneumoniae

Rioux¹,

Neyt²,

Paolo³

et al. 2011

Microbiology

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Restricted to the genus Streptococcus, the Pht protein family comprises four members: PhtA, PhtB, PhtD and PhtE. This family has the potential to provide a protein candidate for incorporation in pneumococcal vaccines. Based on sequence analysis and on RT-PCR experiments, we show here that the pht genes are organized in tandem but that their expression, except that of phtD, is monocistronic. PhtD, PhtE, PhtB and PhtA are present in 100, 97, 81 and 62 % of the strains, respectively, and, by analysing its sequence conservation across 107 pneumococcal strains, we showed that PhtD displays very little variability. To analyse the physiological function of these proteins, several mutants were constructed. The quadruple Pht-deficient mutant was not able to grow in a poor culture medium, but the addition of Zn 2+ or Mn 2+ restored its growth capacity.Moreover, the phtD mRNA expression level increased when the culture medium was depleted in zinc. Therefore, we suggest that these proteins are zinc and manganese scavengers, and are able to store these metals and to release them when the bacterium faces an ion-restricted environment. The data also showed that this protein family, and more particularly PhtD, is a promising candidate to be incorporated into pneumococcal vaccines.

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Characterization Of the Pht Genesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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Transcriptional regulation, occurrence and putative role of the Pht family of Streptococcus pneumoniae

Rioux¹,

Neyt²,

Paolo³

et al. 2011

Microbiology

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Siderophore‐Binding Periplasmatic ProteinFhuDand Related Periplasmic Binding Proteins Involved in Bacterial Iron Uptake

Krewulak

Köster

Vogel

2004

Handbook of Metalloproteins

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To fulfill their nutritional requirement for iron, many microorganisms synthesize low‐molecular‐weight iron‐chelating compounds called siderophores . These iron sources are transported into the gram‐negative bacterial cell via specific uptake pathways that include an outer membrane receptor, a periplasmic binding protein (PBP), and an inner membrane ATP‐binding cassette (ABC) transporter. Gram‐positive bacteria lack an outer membrane, and thus the uptake of the ferric siderophore involves a membrane‐anchored PBP and an ABC transporter. Siderophores are classified as hydroxamate, catecholate, or hydroxycarboxylate type siderophores. This review details what is currently known about the PBP, FhuD (Fhu — ferric hydroxamate uptake), involved in the uptake of hydroxamate‐type siderophores. In addition, several structurally related periplasmic binding proteins that mediate bacterial metal ion transport are also discussed.

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Pneumococcal lipoproteins involved in bacterial fitness, virulence, and immune evasion

et al. 2016

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Edited by Wilhelm JustStreptococcus pneumoniae (pneumococcus) has evolved sophisticated strategies to survive in several niches within the human body either as a harmless commensal or as a serious pathogen causing a variety of diseases. The dynamic interaction between pneumococci and resident host cells during colonization of the upper respiratory tract and at the site of infection is critical for bacterial survival and the development of disease. Pneumococcal lipoproteins are peripherally anchored membrane proteins and have pivotal roles in bacterial fitness including envelope stability, cell division, nutrient acquisition, signal transduction, transport (as substrate-binding proteins of ABC transporter systems), resistance to oxidative stress and antibiotics, and protein folding. In addition, lipoproteins are directly involved in virulence-associated processes such as adhesion, colonization, and persistence through immune evasion. Conversely, lipoproteins are also targets for the host response both as ligands for toll-like receptors and as targets for acquired antibodies. This review summarizes the multifaceted roles of selected pneumococcal lipoproteins and how this knowledge can be exploited to combat pneumococcal infections.

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AdcAII, A New Pneumococcal Zn-Binding Protein Homologous with ABC Transporters: Biochemical and Structural Analysis

Cited by 108 publications

References 57 publications

Transcriptional regulation, occurrence and putative role of the Pht family of Streptococcus pneumoniae

Transcriptional regulation, occurrence and putative role of the Pht family of Streptococcus pneumoniae

Siderophore‐Binding Periplasmatic ProteinFhuDand Related Periplasmic Binding Proteins Involved in Bacterial Iron Uptake

Pneumococcal lipoproteins involved in bacterial fitness, virulence, and immune evasion

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