The Fbe (SdrG) protein of Staphylococcus epidermidis HB promotes bacterial adherence to fibrinogen

Hartford, Orla; O’Brien, Louise; Schofield, Karin; Wells, Jerry M.; Foster, Timothy J.

doi:10.1099/00221287-147-9-2545

Cited by 124 publications

(98 citation statements)

References 35 publications

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“…However, when only the 11 genes encoding putative adhesins were taken into account, the higher prevalence of sdrD in BI isolates than in NC isolates became significant. Some SD proteins were shown to bind fibrinogen (ClfA [21], ClfB [25], and SdrG [16]) or bone sialoprotein (Bbp) (33), but the ability of SdrD to bind a matrix protein(s) has not been investigated. The impact of sdrD inactivation merits evaluation in an animal model of BIs.…”

Section: Discussionmentioning

confidence: 99%

DNA Macroarray for Identification and Typing of Staphylococcus aureus Isolates

et al. 2004

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A DNA macroarray containing 465 intragenic amplicons was designed to identify Staphylococcus aureus at the species level and to type S. aureus isolates. The genes selected included those encoding (i) S. aureus-specific proteins, (ii) staphylococcal and enterococcal proteins mediating antibiotic resistance and factors involved in their expression, (iii) putative virulence proteins and factors controlling their expression, and (iv) proteins produced by mobile elements. The macroarray was hybridized with the cellular DNAs of 80 S. aureus clinical isolates that were previously typed by analyses of their antibiograms and SmaI patterns. The set selected contained unrelated, endemic, and outbreak-related isolates belonging to 45 SmaI genotypes. In a gene content dendrogram, the 80 isolates were distributed into 52 clusters. The outbreak-related isolates were linked in the same or a closely related cluster(s). Clustering based on gene content provided a better discrimination than SmaI pattern analysis for the tested mecA ؉ isolates that were endemic to Europe. All of the antibiotic resistance genes detected could be correlated with their corresponding phenotypes, except for one isolate which carried a mecA gene without being resistant. The 16 isolates responsible for bone infections were distinguishable from the 12 isolates from uninfected nasal carriers by a significantly higher prevalence of the sdrD gene coding for a putative SD (serine-aspartate) adhesin (in 15 and 7 isolates, respectively). In conclusion, the macroarray designed for this study offers an attractive and rapid typing method which has the advantage of providing additional information concerning the gene content of the isolate of interest.The best known staphylococcal species is Staphylococcus aureus, by virtue of its frequent and highly versatile pathogenicity in humans and animals. Isolates belonging to this species are responsible for suppurative infections and syndromes provoked by toxins. Excluding pathologies caused by toxins such as enterotoxins and exfoliative or toxic shock syndrome toxins (20), the pathology of a staphylococcal infection is attributable not to a single factor but to the coordinated actions of several factors whose expression is controlled by several regulatory systems (3,26,29,30). S. aureus is one of the most common causes of nosocomial infections. The emergence of such infections is of particular concern since most isolates, such as methicillin-resistant S. aureus (MRSA), are resistant to several antibiotics (4, 28) and because the spread of these strains in hospitals often increases the overall incidence of nosocomial S. aureus infections in the institution. MRSA clinical isolates with decreased susceptibilities to glycopeptides (1, 17) threaten to compromise our ability to treat hospital-acquired S. aureus infections.S. aureus typing is a useful adjunct in several clinical settings, in addition to its use during dramatic acute outbreaks. Despite the use of several phenotypic and genotypic methods (antibiotyping, phage typi...

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Section: Discussionmentioning

confidence: 99%

DNA Macroarray for Identification and Typing of Staphylococcus aureus Isolates

et al. 2004

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“…Lactococcus lactis MG1363 was used for heterologous expression of SasG (Gasson, 1983). The plasmid expression vector used was pKS80, a derivative of pTREX1 (Hartford et al, 2001;Wells & Scholfield, 1996). L. lactis was grown at 30 uC for 16 h on M17 agar or broth (Difco) containing 0?5 % (w/v) glucose.…”

Section: Methodsmentioning

confidence: 99%

“…The single PCR product was purified, cut with BclI and cloned into the BclI site of the L. lactis expression vector pKS80. The recombinant plasmid was transformed into competent L. lactis MG1363 cells by electroporation as described previously (Hartford et al, 2001;Wells et al, 1993). Transformants were selected on M17 agar containing glucose and erythromycin.…”

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The Staphylococcus aureus surface protein SasG and its homologues promote bacterial adherence to human desquamated nasal epithelial cells

2003

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Staphylococcus aureus binds to human desquamated nasal epithelial cells, a phenomenon likely to be important in nasal colonization. ClfB was identified previously as one staphylococcal adhesin that promoted binding to nasal epithelia. In this study, it is shown that the S. aureus surface protein SasG, identified previously by in silico analysis of genome sequences, and two homologous proteins, Pls of S. aureus and AAP of Staphylococcus epidermidis, also promote bacterial adherence to nasal epithelial cells. Conditions for in vitro expression of SasG by S. aureus were not found. Adherence assays were therefore performed with S. aureus and Lactococcus lactis expressing SasG from an expression plasmid. These studies showed that SasG did not bind several ligands typically bound by S. aureus. Significantly, SasG and Pls did promote bacterial adherence to nasal epithelial cells. Furthermore, pre-incubation of epithelial cells with purified recombinant proteins revealed that the N-terminal A regions of SasG, Pls and AAP, but not the B repeats of SasG, inhibited adherence of L. lactis expressing SasG in a dose-dependent fashion. These results suggest that SasG, Pls and AAP bind to the same as-yet-unidentified receptor on the surface of nasal epithelial cells. In addition, expression of SasG, like Pls, reduced adherence of S. aureus to fibronectin and fibrinogen.

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“…The FnBP's bind fibrinogen via the N1, N2 and N3 domains and fibronectin via the repeat domains (11 in FnBPA and 10 in FnBPB) [58]. SdrG (S. epidermidis) has the same structural organisation as the clumping factors and bind directly to the beta-chain of the fibrinogen molecule with a Kd in the range of 90-300nm [59,60].…”

Section: Indirect Interaction With Gpiibiiiamentioning

confidence: 99%

Platelet Interactions with Bacteria

Kerrigan¹

2015

The Non-Thrombotic Role of Platelets in Health and Disease

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The Fbe (SdrG) protein of Staphylococcus epidermidis HB promotes bacterial adherence to fibrinogen

Cited by 124 publications

References 35 publications

DNA Macroarray for Identification and Typing of Staphylococcus aureus Isolates

DNA Macroarray for Identification and Typing of Staphylococcus aureus Isolates

The Staphylococcus aureus surface protein SasG and its homologues promote bacterial adherence to human desquamated nasal epithelial cells

Platelet Interactions with Bacteria

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