Characterisation and functional aspects of monoclonal antibodies specific for surface proteins of coagulase-negative staphylococci

Timmerman, C. P.; Besnier, Jean-Marc; Graaf, Loek de; Torensma, Ruurd; Verkley, A. J.; Fleer, A.; Verhoef, J.

doi:10.1099/00222615-35-2-65

Cited by 7 publications

(7 citation statements)

References 15 publications

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“…2002), called biofilm, the main known virulence factors of these bacteria. Attachment to the surface is the first step in this process, mediated by cell wall‐anchored proteins, some extracellular enzymes and possibly pili (Timmerman et al. 1991; Banner et al.…”

Section: Discussionmentioning

confidence: 99%

“…The pathogenic process of foreign-body-associated infections is characterized by the ability of these bacteria to colonize polymer surfaces and form a multilayered cell cluster (von Eiff et al 2002), called biofilm, the main known virulence factors of these bacteria. Attachment to the surface is the first step in this process, mediated by cell wall-anchored proteins, some extracellular enzymes and possibly pili (Timmerman et al 1991;Banner et al 2007). The second step is accumulation of the cells to a multilayer as well as the formation of an extracellular matrix, which comprises several polysaccharides, proteins, considerable amounts of teichoic acids and also extracellular DNA.…”

Section: Discussionmentioning

confidence: 99%

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Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation ofStaphylococcus epidermidis

Hell

Giske

Nelson

et al. 2010

Letters in Applied Microbiology

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Aims: The aim of this work was to investigate the possible effect of human cathelicidin antimicrobial peptide LL37 on biofilm formation of Staphylococcus epidermidis, a major causative agent of indwelling device‐related infections. Methods and Results: We performed initial attachment assay and biofilm formation solid surface assay in microtitre plates, as well as growth experiment in liquid medium using laboratory strain Staph. epidermidis ATCC35984. We found that already a low concentration of the peptide LL37 (1 mg l−1) significantly decreased both the attachment of bacteria to the surface and also the biofilm mass. No growth inhibition was observed even at 16 mg l−1 concentration of LL37, indicating a direct effect of the peptide on biofilm production. Conclusions: As biofilm protects bacteria during infections in humans and allows their survival in a hostile environment, inhibition of biofilm formation by LL37 may have a key role to prevent bacterial colonization on indwelling devices. Significance and Impact of the Study: Our findings suggest that this host defence factor can be a potential candidate in prevention and treatment strategies of Staph. epidermidis infections in humans.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation ofStaphylococcus epidermidis

Hell

Giske

Nelson

et al. 2010

Letters in Applied Microbiology

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“…Immunogold assays. Immunogold assays were performed by a modification of the procedure of Timmerman et al (24). In 0.5 ml of 0.5% glutaraldehyde-2% paraformaldehyde in PBS (pH 7.4) and allowed to incubate for 1 h at 22°C.…”

Section: Materuils and Methodsmentioning

confidence: 99%

Characterization of Bartonella bacilliformis flagella and effect of antiflagellin antibodies on invasion of human erythrocytes

1993

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Bartonella bacilliformis is the etiologic agent of Oroya fever in humans. Flagellum-mediated motility has been postulated as a major virulence factor for invasion of host cells. To address this hypothesis, we purified and characterized flagella from strain KC584 and then assessed their role in human erythrocyte association and invasion. Electron microscopy of the flagellar preparation showed a high concentration of filaments with a mean wavelength of 800 nm. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunoblot analysis, and KBr density gradient centrifugation indicated that the flagellar filament is composed of a polypeptide of 42 kDa. The flageHlin is partially (ca. 50%) resistant to treatment with trypsin. The first 17 amino acid residues of the N terminus of the mature flagellin protein are GAAILTNDNAMDALQDL and show approximately 46% sequence identity to the residues of the N termini of two Caulobacter crescentus flagellin proteins. A monospecific polyclonal antibody to the flagellin protein was generated, and its specificity was verified by both immunoblot and immunogold analyses. Human erythrocyte invasion assays performed with bartonellae 4962 on July 16, 2020 by guest http://iai.asm.org/ Downloaded from

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“…The first step is primary adhesion of some bacteria, which is followed by proliferation of the cells to multilayered clusters. Factors reported to contribute to primary attachment of S. epidermidis cells to a polymer surface include unspecific hydrophobic interactions (5,6), a capsular polysaccharide/adhesin (PS/A) (7,8), proteinaceous cell-surface antigens (SSP-1 and SSP-2) (9,10), and the autolysin AtlE identified by our group (11).…”

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confidence: 89%

Characterization of theN-Acetylglucosaminyltransferase Activity Involved in the Biosynthesis of the Staphylococcus epidermidisPolysaccharide Intercellular Adhesin

Gerke¹,

Kraft²,

Süßmuth³

et al. 1998

Journal of Biological Chemistry

426

366

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The polysaccharide intercellular adhesin (PIA) is an important factor in the colonization of medical devices by Staphylococcus epidermidis. The genes encoding PIA production are organized in the icaADBC (intercellular adhesion) operon. To study the function of the individual genes, we have established an in vitro assay with UDP-N-acetylglucosamine, the substrate for PIA biosynthesis, and analyzed the products by thin-layer chromatography and mass spectrometry. IcaA alone exhibited a low N-acetylglucosaminyltransferase activity and represents the catalytic enzyme. Coexpression of icaA with icaD led to a significant increase in activity. The newly identified icaD gene is located between icaA and icaB and overlaps both genes. N-Acetylglucosamine oligomers produced by IcaAD reached a maximal length of 20 residues. Only when icaA and icaD were expressed together with icaC were oligomer chains that react with PIA-specific antiserum synthesized. IcaA and IcaD are located in the cytoplasmic membrane, and IcaC also has all the structural features of an integral membrane protein. These results indicate a close interaction between IcaA, IcaD, and IcaC. Tunicamycin and bacitracin did not affect the in vitro synthesis of PIA intermediates or the complete PIA biosynthesis in vivo, suggesting that a undecaprenyl phosphate carrier is not involved. IcaAD represents a novel protein combination among ␤-glycosyltransferases.In recent years, Staphylococcus epidermidis has emerged as a frequent cause of nosocomial infections in association with indwelling medical devices such as intravascular catheters, cerebrospinal fluid shunts, prosthetic heart valves, prosthetic joints, artificial pacemakers, and chronic ambulatory peritoneal dialysis catheters (reviewed in Refs. 1 and 2). The virulence of S. epidermidis in these infections is thought to be based on its ability to colonize medical devices by forming a biofilm composed of multilayered cell clusters embedded in a slime matrix (3). As shown by electron microscopy studies, surface colonization takes place in two steps (4). The first step is primary adhesion of some bacteria, which is followed by proliferation of the cells to multilayered clusters. Factors reported to contribute to primary attachment of S. epidermidis cells to a polymer surface include unspecific hydrophobic interactions (5, 6), a capsular polysaccharide/adhesin (PS/A) (7, 8), proteinaceous cell-surface antigens (SSP-1 and SSP-2) (9, 10), and the autolysin AtlE identified by our group (11).A characteristic feature of the second phase of biofilm formation is intercellular adhesion, which results in the formation of large cell clusters by clinical S. epidermidis strains. This reaction is associated with the production of the polysaccharide intercellular adhesin (PIA) 1 located at the cell surface (12). PIA consists of two structurally related homoglycans, polysaccharides I and II, composed of at least 130 2-deoxy-2-amino-Dglucopyranosyl residues that are mostly (Ͼ80%) N-acetylated. The residues are ␤-1,6-linked (13), ...

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Characterisation and functional aspects of monoclonal antibodies specific for surface proteins of coagulase-negative staphylococci

Cited by 7 publications

References 15 publications

Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation ofStaphylococcus epidermidis

Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation ofStaphylococcus epidermidis

Characterization of Bartonella bacilliformis flagella and effect of antiflagellin antibodies on invasion of human erythrocytes

Characterization of theN-Acetylglucosaminyltransferase Activity Involved in the Biosynthesis of the Staphylococcus epidermidisPolysaccharide Intercellular Adhesin

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