Characterization of cell envelope proteins of Staphylococcus epidermidis cultured in human peritoneal dialysate

Smith, David G.; Wilcox, Mark H.; Williams, Paul; Finch, Roger; Denyer, Stephen Paul

doi:10.1128/iai.59.2.617-624.1991

Cited by 35 publications

(44 citation statements)

References 30 publications

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“…In both S. aureus and S. epidermidis, a number of cell walland cytoplasmic membrane-associated proteins, the production of which depends on the growth medium iron content, have been identified (6,24,37,45). Of these, we have recently cloned and sequenced an iron-regulated 32-kDa lipoprotein, SitC, which is encoded by a component of the sitABC operon (6).…”

Section: Discussionmentioning

confidence: 99%

“…Although they produce and use siderophores (low-molecular-mass iron chelators), the genes and gene products involved in their regulation, synthesis, export, or import are unknown (44). Previously, we identified a number of iron-repressible S. aureus and S. epidermidis cell wall-and cytoplasmic membrane-associated proteins which are expressed during growth in vivo during both human (37,45) and experimental animal (23,25) infections. These include a 42-kDa cell wall protein which functions as a receptor for human transferrin (24,26) and a 32-kDa cytoplasmic membrane-associated lipoprotein (6,23,37).…”

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confidence: 99%

“…Previously, we identified a number of iron-repressible S. aureus and S. epidermidis cell wall-and cytoplasmic membrane-associated proteins which are expressed during growth in vivo during both human (37,45) and experimental animal (23,25) infections. These include a 42-kDa cell wall protein which functions as a receptor for human transferrin (24,26) and a 32-kDa cytoplasmic membrane-associated lipoprotein (6,23,37). The gene encoding this lipoprotein has recently been cloned from S. epidermidis and shown to be a component of a translationally coupled, iron-regulated operon which consists of three genes (sitABC), the products of which constitute an ABC transporter (6).…”

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SirR, a Novel Iron-Dependent Repressor in Staphylococcus epidermidis

et al. 1998

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In Staphylococcus epidermidis and Staphylococcus aureus, a number of cell wall-and cytoplasmic membraneassociated lipoproteins are induced in response to iron starvation. To gain insights into the molecular basis of iron-dependent gene regulation in the staphylococci, we sequenced the DNA upstream of the 3-kb S. epidermidis sitABC operon, which Northern blot analysis indicates is transcriptionally regulated by the growth medium iron content. We identified two DNA sequences which are homologous to elements of the Corynebacterium diphtheriae DtxR regulon, which controls, in response to iron stress, for example, production of diphtheria toxin, siderophore, and a heme oxygenase. Upstream of the sitABC operon and divergently transcribed lies a 645-bp open reading frame (ORF), which codes for a polypeptide of approximately 25 kDa with homology to the DtxR family of metal-dependent repressor proteins. This ORF has been designated SirR (staphylococcal iron regulator repressor). Within the sitABC promoter/operator region, we also located a region of dyad symmetry overlapping the transcriptional start of sitABC which shows high homology to the DtxR operator consensus sequence, suggesting that this region, termed the Sir box, is the SirR-binding site. The SirR protein was overexpressed, purified, and used in DNA mobility shift assays; SirR retarded the migration of a synthetic oligonucleotide based on the Sir box in a metal (Fe 2؉ or Mn 2؉ )-dependent manner, providing confirmatory evidence that this motif is the SirR-binding site. Furthermore, Southern blot analysis of staphylococcal chromosomal DNA with the synthetic Sir box as a probe confirmed that there are at least five Sir boxes in the S. epidermidis genome and at least three in the genome of S. aureus, suggesting that SirR controls the expression of multiple target genes. Using a monospecific polyclonal antibody raised against SirR to probe Western blots of whole-cell lysates of S. aureus, S. carnosus, S. epidermidis, S. hominis, S. cohnii, S. lugdunensis, and S. haemolyticus, we identified an approximately 25-kDa cross-reactive protein in each of the staphylococcal species examined. Taken together, these data suggest that SirR functions as a divalent metal cation-dependent transcriptional repressor which is widespread among the staphylococci.

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SirR, a Novel Iron-Dependent Repressor in Staphylococcus epidermidis

et al. 1998

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“…This chelator could be detected in growth medium supernatants of numerous different staphylococci. The occurrence of iron-regulated membrane proteins in Staphylococcus aureus and Staphylococcus epidermidis was demonstrated by several groups [8][9][10]• Naidu et al [11] identified a specific receptor for human lactoferrin in Staphylococcus aureus, which is assumed to contribute to the iron supply of these strains• Here we describe the isolation and biological properties of a second iron-regulated metabolite found in staphylococci, a compound we called staphyloferrin B.…”

Section: Introductionmentioning

confidence: 90%

Isolation and biological characterization of staphyloferrin B, a compound with siderophore activity from staphylococci

Haag

1994

FEMS Microbiology Letters

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A highly hydrophilic compound with siderophore activity has been isolated from the supernatant of Staphylococcus hyicus DSM 20459 grown under iron-restricted conditions. The metabolite, named staphyloferrin B, is strictly iron-regulated and produced by a large variety of staphylococci strains. In vivo iron transport measurements and the growth-promoting activity in a bioassay establish staphyloferrin B as the second siderophore for staphylococci besides the previously described staphyloferrin A. The structure elucidation revealed 2,3-diaminopropionic acid, citrate, ethylenediamine and 2-ketoglutaric acid as structural components of the compound. Thus, staphyloferrin B is a structurally new siderophore of the complexone type.

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“…Our previous studies identified a number of iron-regulated S. aureus and S. epidermidis proteins, which are expressed in vivo both during human infection (30,35) and in an experimental animal model (23,25). To date, only two of these proteins have been characterized.…”

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Molecular Cloning and Analysis of a Putative Siderophore ABC Transporter from Staphylococcus aureus

2000

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From a mass-excised Staphylococcus aureusZapII expression library, we cloned an operon encoding a novel ABC transporter with significant homology to bacterial siderophore transporter systems. The operon encodes four genes designated sstA, -B, -C, and -D encoding two putative cytoplasmic membrane proteins (sstA and sstB), an ATPase (sstC), and a membrane-bound 38-kDa lipoprotein (sstD). The sst operon is preceded by two putative Fur boxes, which indicated that expression of the sst operon was likely to be iron dependent. SstD was overexpressed in Escherichia coli, purified by Triton X-114 phase partitioning, and used to generate monospecific antisera in rats. Immunoblotting studies located SstD in the membrane fraction of S. aureus and showed that expression of the lipoprotein was reduced under iron-rich growth conditions. Triton X-114 partitioning studies on isolated membranes provided additional biochemical evidence that SstD in S. aureus is a lipoprotein. Immunoreactive polypeptides of approximately 38 kDa were detected in a wide range of staphylococcal species, but no antigenic homolog was detected in Bacillus subtilis. Expression of SstD in vivo was confirmed by immunoblotting studies with S. aureus recovered from a rat intraperitoneal chamber implant model. To further define the contribution of SstD in promoting growth of S. aureus in vitro and in vivo, we used antisense RNA technology to modulate expression of SstD. Expression of antisense sstD RNA in S. aureus resulted in a decrease in SstD expression under both iron-rich and iron-restricted growth conditions. However, this reduction in SstD levels did not affect the growth of S. aureus in vitro in an iron-limited growth medium or when grown in an intraperitoneal rat chamber implant model in vivo.

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Characterization of cell envelope proteins of Staphylococcus epidermidis cultured in human peritoneal dialysate

Cited by 35 publications

References 30 publications

SirR, a Novel Iron-Dependent Repressor in Staphylococcus epidermidis

SirR, a Novel Iron-Dependent Repressor in Staphylococcus epidermidis

Isolation and biological characterization of staphyloferrin B, a compound with siderophore activity from staphylococci

Molecular Cloning and Analysis of a Putative Siderophore ABC Transporter from Staphylococcus aureus

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