Pathogenic Implication of a Fibrinogen-Binding Protein of Staphylococcus epidermidis in a Rat Model of Intravascular-Catheter-Associated Infection

ABSTRACT The involvement of Fbe, a fibrinogen-binding protein of Staphylococcus epidermidis, in the pathogenesis of catheter-associated infection was investigated. An fbe (gene encoding Fbe protein) mutant was constructed by allelic replacement, wherein an erythromycin resistance gene replaced a portion of the A region of fbe. Meanwhile, a rat central venous catheter (CVC) infection model was established to assess the importance of Fbe in the pathogenesis of CVC-associated infection due to S. epidermidis. Fbe-positive S. epidermidis strain HB was significantly more likely to cause a CVC-associated infection resulting in bacteremia and metastatic disease than its isogenic Fbe-deficient mutant (100% versus 20%, P < 0.01). These results confirm the importance of adherence associated with Fbe in the pathogenesis of CVC-associated infection caused by S. epidermidis.

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Characterization of Staphylococcus epidermidisPolysaccharide Intercellular Adhesin/Hemagglutinin in the Pathogenesis of Intravascular Catheter-Associated Infection in a Rat Model

Infection and Immunity ◽

10.1128/iai.67.5.2656-2659.1999 ◽

1999 ◽

Vol 67 (5) ◽

pp. 2656-2659 ◽

Cited By ~ 169

Author(s):

Mark E. Rupp ◽

Joseph S. Ulphani ◽

Paul D. Fey ◽

Dietrich Mack

Keyword(s):

Central Venous Catheter ◽

Staphylococcus Epidermidis ◽

Venous Catheter ◽

Infection Model ◽

Polysaccharide Intercellular Adhesin ◽

Intravascular Catheter ◽

Central Venous ◽

Biofilm Production ◽

Negative Mutant

ABSTRACT Biofilm production is thought to be a crucial factor in the ability of Staphylococcus epidermidis to produce a biomaterial-based infection. A rat central venous catheter (CVC)-associated infection model was used to assess the importance of biofilm production, mediated by polysaccharide intercellular adhesin/hemagglutinin (PIA/HA), in the pathogenesis of intravascular catheter-associated infection. PIA/HA-positive S. epidermidis 1457 was significantly more likely to cause a CVC-associated infection (71 versus 14%, P < 0.03) resulting in bacteremia and metastatic disease than its isogenic PIA/HA-negative mutant. These results confirm the importance of biofilm production, mediated by PIA/HA, in the pathogenesis of S. epidermidis experimental CVC-associated infection.

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Conversion of Staphylococcus epidermidis Strains from Commensal to Invasive by Expression of the ica Locus Encoding Production of Biofilm Exopolysaccharide

Infection and Immunity ◽

10.1128/iai.73.5.3188-3191.2005 ◽

2005 ◽

Vol 73 (5) ◽

pp. 3188-3191 ◽

Cited By ~ 65

Author(s):

Hualin Li ◽

Lin Xu ◽

Jianping Wang ◽

Yumei Wen ◽

Cuong Vuong ◽

...

Keyword(s):

Central Venous Catheter ◽

Staphylococcus Epidermidis ◽

Biofilm Formation ◽

Venous Catheter ◽

Infection Model ◽

Polysaccharide Intercellular Adhesin ◽

Central Venous ◽

Biofilm Production ◽

Central Venous Catheter Infection

ABSTRACT To test if biofilm formation in Staphylococcus epidermidis is dependent on the polysaccharide intercellular adhesin, whose biosynthesis is driven by the ica locus, a plasmid containing the ica locus was transferred to three ica-negative strains. Using in vitro biofilm assays and a rat central venous catheter infection model, we confirmed the importance of the ica locus for biofilm production and pathogenesis of S. epidermidis.

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Functional Studies of a Fibrinogen Binding Protein from Staphylococcus epidermidis

Infection and Immunity ◽

10.1128/iai.67.9.4525-4530.1999 ◽

1999 ◽

Vol 67 (9) ◽

pp. 4525-4530 ◽

Cited By ~ 47

Author(s):

Lei Pei ◽

Marco Palma ◽

Martin Nilsson ◽

Bengt Guss ◽

Jan-Ingmar Flock

Keyword(s):

Nucleotide Sequence ◽

Cell Surface ◽

Staphylococcus Epidermidis ◽

Binding Protein ◽

Enzyme Linked Immunosorbent Assay ◽

Gene Encoding ◽

Functional Studies ◽

Fibrinogen Binding ◽

Associated Proteins ◽

Β Chain

ABSTRACT A gene encoding a fibrinogen binding protein fromStaphylococcus epidermidis was previously cloned, and the nucleotide sequence was determined. A portion of the gene encompassing the fibrinogen binding domain has now been subcloned in an expression-fusion vector. The fusion protein can bind to fibrinogen in a capture enzyme-linked immunosorbent assay and can be purified by fibrinogen affinity chromatography. This protein can completely inhibit the adherence of S. epidermidis to immobilized fibrinogen, suggesting that the adherence of S. epidermidis to fibrinogen is mainly due to this protein. Antibodies against this fibrinogen binding protein were also found to efficiently block the adherence of S. epidermidis to immobilized fibrinogen. Despite homology with clumping factors A and B from S. aureus (cell surface-associated proteins binding to fibrinogen), binding involved the β chain of fibrinogen rather than the γ chain, as in clumping factor A.

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Molecular epidemiology of catheter-related bloodstream infections caused by coagulase-negative staphylococci in haematological patients with neutropenia

Epidemiology and Infection ◽

10.1017/s0950268804002584 ◽

2004 ◽

Vol 132 (5) ◽

pp. 921-925 ◽

Cited By ~ 9

Author(s):

M. MÜLLER-PREMRU ◽

P. ČERNELČ

Keyword(s):

Blood Culture ◽

Staphylococcus Epidermidis ◽

Clinical Signs ◽

Bloodstream Infections ◽

Venous Catheter ◽

Blood Cultures ◽

Peripheral Vein ◽

Central Venous ◽

Coagulase Negative Staphylococci ◽

Haematological Patients

Catheter-related bloodstream infection (CRBSI) caused by coagulase-negative staphylococci (CNS) is common in haematological patients with febrile neutropenia. As the clinical signs of CRBSI are usually scarce and it is difficult to differentiate from blood culture contamination, we tried to confirm CRBSI by molecular typing of CNS isolated from paired blood cultures (one from a peripheral vein and another from the central venous catheter hub). Blood cultures were positive in 59 (36%) out of 163 patients. CNS were isolated in 24 (40%) patients; in 14 from paired blood cultures (28 isolates) and in 10 from a single blood culture. CNS from paired blood cultures were identified as Staphylococcus epidermidis. Antimicrobial susceptibility was determined and bacteria were typed by pulsed-field gel electrophoresis (PFGE) of bacterial genomic DNA. In 13 patients, the antibiotic susceptibility of isolates was identical. The PFGE patterns from paired blood cultures were identical or closely related in 10 patients, thus confirming the presence of CRBSI. In the remaining four patients they were unrelated, and suggested a mixed infection or contamination. Since CNS isolates from three patients had identical PFGE patterns, they were probably nosocomially spread amongst them.

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The Gene Encoding the Low-Affinity Penicillin-Binding Protein 3r in Enterococcus hirae S185R Is Borne on a Plasmid Carrying Other Antibiotic Resistance Determinants

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.42.3.534 ◽

1998 ◽

Vol 42 (3) ◽

pp. 534-539 ◽

Cited By ~ 28

Author(s):

Dominique Raze ◽

Olivier Dardenne ◽

Séverine Hallut ◽

Manuel Martinez-Bueno ◽

Jacques Coyette ◽

...

Keyword(s):

Binding Protein ◽

Bacterial Species ◽

Multidrug Resistant ◽

Penicillin Binding Protein ◽

Enterococcus Hirae ◽

Erythromycin Resistance ◽

Gene Encoding ◽

Transposase Gene ◽

Encoding Gene ◽

High Degree

ABSTRACT Two plasmid-derived NcoI DNA fragments of 14 and 4.5 kb, respectively, have been isolated from the multidrug-resistant strain Enterococcus hirae S185R and analyzed. The 14-kb fragment contains two inverted (L and R) IS1216 insertion modules of the ISS1 family. These modules define a Tn5466 transposon-like structure that contains one copy of the methylase-encoding ermAMconferring erythromycin resistance and one copy of the adenylyl-transferase-encoding aadE conferring streptomycin resistance. Immediately on the left side of IS1216L there occurs a copy of pbp3r encoding the low-affinity penicillin-binding protein (PBP) PBP3r, itself preceded by apsr-like gene (psr3r) that controls the synthesis of PBP3r. ermAM, aadE, and the transposase gene (tnp) of IS1216R have the same polarities, and these are opposite those of psr3r,pbp3r, and the tnp gene of IS1216L. The 4.5-kb fragment is a copy of the 4.5-kb sequence at the 5′ end of the 14-kb fragment, although it is not a restriction product of the 14-kb fragment. It contains three genes with the same polarity:psr3r, pbp3r, and tnp in an IS1216 element. Because of the very high degree of identity (99%) with the chromosomal psrfm and pbp5fmgenes of Enterococcus faecium D63R, it is proposed that both the psr3r and pbp3r genes were transferred from an E. faecium strain and inserted in a plasmid ofE. hirae. E. hirae is the first known bacterial species in which a low-affinity PBP-encoding gene has been found to be plasmid borne.

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Identification of a Fibronectin-Binding Protein from Staphylococcus epidermidis

Infection and Immunity ◽

10.1128/iai.70.12.6805-6810.2002 ◽

2002 ◽

Vol 70 (12) ◽

pp. 6805-6810 ◽

Cited By ~ 108

Author(s):

Rachel J. Williams ◽

Brian Henderson ◽

Lindsay J. Sharp ◽

Sean P. Nair

Keyword(s):

Recombinant Protein ◽

Staphylococcus Epidermidis ◽

Binding Protein ◽

Phage Display Library ◽

Binding Domain ◽

Genomic Research ◽

Gene Encoding ◽

Reading Frame ◽

Fibronectin Binding Protein ◽

Fibronectin Binding

ABSTRACT Staphylococcus epidermidis has been reported to bind to a number of host cell extracellular matrix proteins, including fibronectin. Here we report the identification of a fibronectin-binding protein from S. epidermidis. A phage display library of S. epidermidis genomic DNA was constructed and panned against immobilized fibronectin. A number of phagemid clones containing overlapping inserts were identified, and one of these clones, pSE109FN, contained a 1.4-kb insert. Phage pSE109FN was found to bind to fibronectin but not to collagen, fibrinogen, laminin, or vitronectin. However, pSE109FN also bound to heparin, hyaluronate, and plasminogen, although to a lesser extent than it bound to fibronectin. Analysis of The Institute for Genomic Research S. epidermidis genome sequence database revealed a 1.85-kb region within a putative 30.5-kb open reading frame, to which the overlapping DNA inserts contained within the fibronectin-binding phagemids mapped. We have designated the gene encoding the fibronectin-binding domain embp. A recombinant protein, Embp32, which encompassed the fibronectin-binding domain of Embp, blocked the binding of S. epidermidis, but not the binding of Staphylococcus aureus, to fibronectin. In contrast, a recombinant protein, FnBPB[D1-D4], spanning the fibronectin-binding domain of the S. aureus fibronectin-binding protein FnBPB, blocked binding of S. aureus to fibronectin but had a negligible effect on the binding of S. epidermidis.

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Lack of fbe, the gene for a fibrinogen-binding protein from Staphylococcus epidermidis, reduces its adherence to fibrinogen coated surfaces

Microbial Pathogenesis ◽

10.1006/mpat.2001.0462 ◽

2001 ◽

Vol 31 (4) ◽

pp. 185-193 ◽

Cited By ~ 36

Author(s):

Lei Pei ◽

Jan-Ingmar Flock

Keyword(s):

Staphylococcus Epidermidis ◽

Binding Protein ◽

Fibrinogen Binding ◽

Coated Surfaces

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Analysis of different genetic traits and their association with biofilm formation in Staphylococcus epidermidis isolates from central venous catheter infections

European Journal of Clinical Microbiology & Infectious Diseases ◽

10.1007/s10096-006-0226-8 ◽

2006 ◽

Vol 25 (12) ◽

pp. 773-781 ◽

Cited By ~ 33

Author(s):

D. Petrelli ◽

C. Zampaloni ◽

S. D’Ercole ◽

M. Prenna ◽

P. Ballarini ◽

...

Keyword(s):

Central Venous Catheter ◽

Staphylococcus Epidermidis ◽

Biofilm Formation ◽

Venous Catheter ◽

Central Venous ◽

Genetic Traits ◽

Catheter Infections

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First Report of Antimicrobial Susceptibility and Virulence Gene Characterization Associated with Staphylococcus aureus Carriage in Healthy Camels from Tunisia

Animals ◽

10.3390/ani11092754 ◽

2021 ◽

Vol 11 (9) ◽

pp. 2754

Author(s):

Faten Ben Chehida ◽

Haythem Gharsa ◽

Wafa Tombari ◽

Rachid Selmi ◽

Sana Khaldi ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Binding Protein ◽

Rectal Mucosa ◽

Virulence Gene ◽

Spa Typing ◽

Gene Encoding ◽

Gene Characterization ◽

Molecular Tests ◽

Fibrinogen Binding ◽

Laminin Binding Protein

A total of 318 nasal and rectal swabs were collected from 159 apparently healthy camels (Camelus dromedarius) randomly selected from five regions in southern and central Tunisia and screened for Staphylococcus aureus carriage. Staphylococcus spp. were recovered from 152 of 159 camels studied (95.6%) and in total 258 swabs (81%) were positive. Among these isolates, 16 were coagulase positive Staphylococcus (CoPS) (6.2%) and were characterized by biochemical and molecular tests as S. aureus. These were isolated from 14 camels (8.8%) with co-carriage in nasal and rectal mucosa by two camels. All S. aureus isolates recovered were methicillin-susceptible Staphylococcus aureus (MSSA) and were characterized by spa typing and PFGE. Three different spa types were recovered: t729, t4013 and a spa type newly registered as t19687, which was the most common. PFGE analysis revealed seven different patterns and these were characterized by MLST, which revealed five different sequence types (ST6, ST88, ST3583 and two new sequences, ST6504 and ST6506). All isolates harbored different virulence genes, including hld, encoding delta hemolysin; lukE–lukD, encoding bicomponent leukotoxin LukE–LukD; the clfB gene, encoding clumping factor B; the laminin gene, encoding laminin-binding protein; and cap8, encoding capsule type 8. Fifteen isolates harbored hemolysin beta (hlb) and fourteen encoded hemolysin alpha (hla) and hemolysin G2 (hlgv). Adhesin factors, including clfA and fnbB, were detected in five and four isolates respectively. Binding proteins, including collagen (cbp) and elastin-binding protein (ebp), were detected in two S. aureus isolates while fibrinogen-binding protein (fib) was identified in four isolates. This study provides the first set of genotyping data on the population structure and presence of toxin genes of S. aureus strains in Tunisian camels.

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