SdrF, a Staphylococcus epidermidis Surface Protein, Binds Type I Collagen

Arrecubieta, Carlos; Lee, Mei-Ho; Macey, Alistair R. M.; Foster, Timothy J.; Lowy, Franklin D.

doi:10.1074/jbc.m610940200

Cited by 82 publications

(102 citation statements)

References 43 publications

(37 reference statements)

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“…Nine of these proteins were proteins with an LPXTG motif (4,12). Five LPXTG motif-containing proteins (Aap, Bhp, SdrF, SdrG, and SesI) are known to play important roles in the pathogenesis of S. epidermidis infections (2,8,10,14,30). In publicly available genomes of S. epidermidis strains RP62A and ATCC 12228, respectively, 11 and 10 genes encoding LPXTG motif-containing proteins have been identified (4), including …”

Section: Discussionmentioning

confidence: 99%

Vaccination with SesC Decreases Staphylococcus epidermidis Biofilm Formation

et al. 2012

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ABSTRACTThe increased use of medical implants has resulted in a concomitant rise in device-related infections. The majority of these infections are caused byStaphylococcus epidermidisbiofilms. Immunoprophylaxis and immunotherapy targetingin vivo-expressed, biofilm-associated, bacterial cell surface-exposed proteins are promising new approaches to prevent and treat biofilm-related infections, respectively. Using anin silicoprocedure, we identified 64 proteins that are predicted to beS.epidermidissurface exposed (Ses), of which 36 were annotated as (conserved) hypothetical. Of these 36 proteins, 5 proteins—3 LPXTG motif-containing proteins (SesL, SesB, and SesC) and 2 of the largest ABC transporters (SesK and SesM)—were selected for evaluation as vaccine candidates. This choice was based on protein size, number of antigenic determinants, or the established role inS. epidermidisbiofilm formation of the protein family to which the candidate protein belongs. Anti-SesC antibodies exhibited the greatest inhibitory effect onS. epidermidisbiofilm formationin vitroand on colonization and infection in a mouse jugular vein catheter infection model that includes biofilms and organ infections. Active vaccination with a recombinant truncated SesC inhibitedS. epidermidisbiofilm formation in a rat model of subcutaneous foreign body infection. Antibodies to SesC were shown to be opsonic by anin vitroopsonophagocytosis assay. We conclude that SesC is a promising target for antibody mediated strategies againstS. epidermidisbiofilm formation.

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Section: Discussionmentioning

confidence: 99%

Vaccination with SesC Decreases Staphylococcus epidermidis Biofilm Formation

et al. 2012

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“…Collectively, our data suggest Aap is a bifunctional biofilm matrix protein, with the A domain mediating initial attachment and the B domain facilitating cell accumulation. This is not unprecedented, as dual-function proteins have been identified in S. epidermidis and other species (14,(102)(103)(104)(105). Additional studies are needed to define the cleavage dynamics of Aap and the corresponding contribution to biofilm formation and virulence of S. epidermidis.…”

Section: Figmentioning

confidence: 99%

Accumulation-Associated Protein Enhances Staphylococcus epidermidis Biofilm Formation under Dynamic Conditions and Is Required for Infection in a Rat Catheter Model

et al. 2015

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Biofilm formation is the primary virulence factor of Staphylococcus epidermidis. S. epidermidis biofilms preferentially form on abiotic surfaces and may contain multiple matrix components, including proteins such as accumulation-associated protein (Aap). Following proteolytic cleavage of the A domain, which has been shown to enhance binding to host cells, B domain homotypic interactions support cell accumulation and biofilm formation. To further define the contribution of Aap to biofilm formation and infection, we constructed an aap allelic replacement mutant and an icaADBC aap double mutant. When subjected to fluid shear, strains deficient in Aap production produced significantly less biofilm than Aap-positive strains. To examine the in vivo relevance of our findings, we modified our previously described rat jugular catheter model and validated the importance of immunosuppression and the presence of a foreign body to the establishment of infection. The use of our allelic replacement mutants in the model revealed a significant decrease in bacterial recovery from the catheter and the blood in the absence of Aap, regardless of the production of polysaccharide intercellular adhesin (PIA), a well-characterized, robust matrix molecule. Complementation of the aap mutant with full-length Aap (containing the A domain), but not the B domain alone, increased initial attachment to microtiter plates, as did in trans expression of the A domain in adhesion-deficient Staphylococcus carnosus. These results demonstrate Aap contributes to S. epidermidis infection, which may in part be due to A domain-mediated attachment to abiotic surfaces.

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“…The expect values were between 1 ϫ 10 Ϫ30 and 4 ϫ 10 Ϫ118 , suggesting a probable phylogenetic relatedness of Srr-1 with these proteins. Members of the Clf-Sdr family typically exhibit adhesive functions and are thus described to bind fibrinogen, collagen, bone sialoprotein, or K10 (4,15,38,40,42,48,63).…”

Section: Sequence Analysis Of the Srr-1-encoding Regionmentioning

confidence: 99%

The Surface Protein Srr-1 of Streptococcus agalactiae Binds Human Keratin 4 and Promotes Adherence to Epithelial HEp-2 Cells

et al. 2007

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Streptococcus agalactiae is frequently the cause of bacterial sepsis and meningitis in neonates. In addition, it is a commensal bacterium that colonizes the mammalian gastrointestinal tract. During its commensal and pathogenic lifestyles, S. agalactiae colonizes and invades a number of host compartments, thereby interacting with different host proteins. In the present study, the serine-rich repeat protein Srr-1 from S. agalactiae was functionally investigated. Immunofluorescence microscopy showed that Srr-1 was localized on the surface of streptococcal cells. The Srr-1 protein was shown to interact with a 62-kDa protein in human saliva, which was identified by matrix-assisted laser desorption ionization-time-of-flight analysis as human keratin 4 (K4). Immunoblot and enzyme-linked immunosorbent assay experiments allowed us to narrow down the K4 binding domain in Srr-1 to a region of 157 amino acids (aa). Furthermore, the Srr-1 binding domain of K4 was identified in the C-terminal 255 aa of human K4. Deletion of the srr-1 gene in the genome of S. agalactiae revealed that this gene plays a role in bacterial binding to human K4 and that it is involved in adherence to epithelial HEp-2 cells. Binding to immobilized K4 and adherence to HEp-2 cells were restored by introducing the srr-1 gene on a shuttle plasmid into the srr-1 mutant. Furthermore, incubation of HEp-2 cells with the K4 binding domain of Srr-1 blocked S. agalactiae adherence to epithelial cells in a dose-dependent fashion. This is the first report describing the interaction of a bacterial protein with human K4.

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SdrF, a Staphylococcus epidermidis Surface Protein, Binds Type I Collagen

Cited by 82 publications

References 43 publications

Vaccination with SesC Decreases Staphylococcus epidermidis Biofilm Formation

Vaccination with SesC Decreases Staphylococcus epidermidis Biofilm Formation

Accumulation-Associated Protein Enhances Staphylococcus epidermidis Biofilm Formation under Dynamic Conditions and Is Required for Infection in a Rat Catheter Model

The Surface Protein Srr-1 of Streptococcus agalactiae Binds Human Keratin 4 and Promotes Adherence to Epithelial HEp-2 Cells

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