A collagen receptor on <i>Staphylococcus aureus</i> strains isolated from patients with septic arthritis mediates adhesion to cartilage

Switalski, Lech M.; Patti, Joseph M.; Butcher, Wade G.; Gristina, Anthony G.; Speziale, Pietro; Höök, Magnus

doi:10.1111/j.1365-2958.1993.tb01101.x

Cited by 196 publications

(135 citation statements)

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“…For example, the collagen-binding adhesin (Cna) is present in only 32 % of carriage isolates but is found in 52 % of isolates from invasive disease (Peacock et al, 2002). An earlier study suggested an association between cna and septic arthritis (Switalski et al, 1993). In this study, the sasG and sasH genes were found to be virulence-associated genes; genes encoding the surface proteins FnbpA, Cna and SdrE were previously found to be virulence-associated in the same panel of invasive strains, indicating the important role played by some of the surface-expressed proteins in disease pathogenesis (Peacock et al, 2002).…”

Section: Discussionmentioning

confidence: 66%

Characterization of novel LPXTG-containing proteins of Staphylococcus aureus identified from genome sequences

et al. 2003

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Section: Discussionmentioning

confidence: 66%

Characterization of novel LPXTG-containing proteins of Staphylococcus aureus identified from genome sequences

et al. 2003

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“…The collagen adhesin of S. aureus is a virulence factor in experimental bacterial arthritis and osteomyelitis (19). We now report that a contact lens-associated ulcerative keratitis model can be used to investigate the dynamics of bacterial adherence to the injured corneal surface.…”

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confidence: 99%

The Collagen-Binding Adhesin Is a Virulence Factor in Staphylococcus aureus Keratitis

Rhem

Lech

Patti³

et al. 2000

Infect Immun

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A collagen-binding strain of Staphylococcus aureus produced suppurative inflammation in a rabbit model of soft contact lens-associated bacterial keratitis more often than its collagen-binding-negative isogenic mutant. Reintroduction of the cna gene on a multicopy plasmid into the mutant helped it regain its corneal adherence and infectivity. The topical application of a collagen-binding peptide before bacterial challenge decreased S. aureus adherence to deepithelialized corneas. These data suggest that the collagen-binding adhesin is involved in the pathogenesis of S. aureus infection of the cornea.Our understanding of the pathogenesis of infectious diseases of the eye is emerging. The intact ocular surface thwarts most microorganisms, but predisposing factors such as contact lens wear can expose tissue components conducive to bacterial adhesion. A breakdown in local defenses and a source of microbial contaminants increase the risk of eye infection.Staphylococcus aureus is responsible for many types of human ocular infections (21) and accounts for 10% of culturepositive microbial keratitis at our institution. S. aureus adheres to the injured cornea (12) and releases proteins that disrupt corneal tissue (11).S. aureus possesses a family of adhesins that are localized at the microbial surface and that interact with extracellular matrix components such as collagen, fibronectin, fibrinogen, laminin, and elastin with high affinity and specificity (4, 13). One staphylococcal adhesin is composed of an N-terminal domain with a collagen-binding site and an antipodal domain that attaches to the bacterial cell wall and projects into the cytoplasm (16). We sought to determine whether a rift in the corneal epithelial surface would increase the risk of corneal adherence and infection by collagen-binding S. aureus.Previous animal models of staphylococcal keratitis used direct intrastromal injection to infect the cornea (1, 2, 5, 7, 9). However, direct inoculation into the corneal stroma does not allow the investigation of bacterial adherence to the corneal surface, a critical initial event in the pathogenesis of microbial keratitis. Because staphylococci attach to contact lenses (3), an animal model using soft contact lenses contaminated with S. aureus was developed to study the role of bacterial adherence in the initiation of keratitis. To enhance the risk of infection, we applied a high-inoculum challenge to surface-injured corneas. This model was then used to study the biological role of the collagen-binding adhesin in S. aureus keratitis by comparing the levels of virulence of a parental strain (Cna ϩ ), its isogenic mutant (Cna Ϫ ), and the isogenic mutant complemented with an intact version of the gene (cna) encoding the collagen-binding adhesin. We also studied the protective effect of applying adhesin analogs before bacterial challenge.Rabbit model of S. aureus keratitis. The animals used in this study were treated according to the criteria of the Association for Research in Vision and Ophthalmology Resolution on the U...

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“…The importance of the MSCRAMM proteins to the virulence of S. aureus has been demonstrated by studying isogenic mutants in animal models of infection. The collagen-binding protein, Cna, was implicated in the pathogenesis of osteomyelitis and septic arthritis (1,6,7), and the fibrinogen-binding protein, ClfA, promoted experimental endocarditis (8) and septic arthritis (9).…”

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confidence: 99%

“…Staphylococcus aureus is a human pathogen that can express several proteins on its cell surface that promote bacterial adherence to proteins of the mammalian extracellular matrix (ECM). 1 Collectively, these proteins are called microbial surface components recognizing adhesive matrix molecules (MSCRAMMs). The binding to the ECM allows bacteria to adhere to and colonize the host tissue.…”

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The N-terminal A Domain of Fibronectin-binding Proteins A and B Promotes Adhesion of Staphylococcus aureus to Elastin

Roche

Downer

Keane

et al. 2004

Journal of Biological Chemistry

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The ability of Staphylococcus aureus to adhere to components of the extracellular matrix is an important mechanism for colonization of host tissues during infection. We have previously shown that S. aureus binds elastin, a major component of the extracellular matrix. The integral membrane protein, elastin-binding protein (EbpS), binds soluble elastin peptides and tropoelastin via its surface-exposed N-terminal domain. In this study, we demonstrate that some strains of S. aureus adhere strongly to immobilized human elastin and that this interaction is independent of EbpS but instead is mediated by the fibronectin-binding proteins, FnBPA and FnBPB. Our results show that EbpS mutant cells adhere to elastin-coated plates, whereas the cells negative for FnBPA and FnBPB do not adhere to the plates. Furthermore, only wild-type cells from the exponential phase of growth adhered when FnBPs were expressed maximally. We show that adherence to elastin promoted by FnBPA was not affected by soluble fibronectin, suggesting that the elastin binding domain is distinct from the fibronectin binding regions. Recombinant FnBPA 37-544 (rFnBPA 37-544 ) protein corresponding to the A region of FnBPA and anti-FnBPA 37-544 antibodies inhibited FnBPA-mediated bacterial adherence to immobilized elastin. Finally, recombinant A domain proteins, rFnBPA 37-544 and rFnBPB 37-540 , bound immobilized elastin dose-dependently and saturably. This interaction was inhibited by soluble elastin peptides, suggesting a specific receptor-ligand interaction.

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A collagen receptor on Staphylococcus aureus strains isolated from patients with septic arthritis mediates adhesion to cartilage

Cited by 196 publications

References 23 publications

Characterization of novel LPXTG-containing proteins of Staphylococcus aureus identified from genome sequences

Characterization of novel LPXTG-containing proteins of Staphylococcus aureus identified from genome sequences

The Collagen-Binding Adhesin Is a Virulence Factor in Staphylococcus aureus Keratitis

The N-terminal A Domain of Fibronectin-binding Proteins A and B Promotes Adhesion of Staphylococcus aureus to Elastin

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