Specific Binding of Collagen to Staphylococcus Aureus

Holderbaum, Daniel; Spech, Richard A.; Ehrhart, L A

doi:10.1016/s0174-173x(85)80016-9

Cited by 55 publications

(38 citation statements)

References 17 publications

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“…The type V collagen-binding sites on the 48-kDa and 65-kDa polypeptides, both different from the Ph or the 110-kDa polypeptide, might be damaged by heat treatment, resulting in no detection in the heated preparation. Immunoglobulin G, fibronectin, fibrinogen and complement do not seem to interfere with the collagen-binding of bacteria (6). The competitive experiment also showed no effect of the type III and IV collagens on the binding of the Ph to the type V collagen.…”

Section: Discussionmentioning

confidence: 77%

Binding of Host‐Associated Treponeme Proteins to Collagens and Laminin: A Possible Mechanism of Spirochetal Adherence to Host Tissues

Umemoto

Namikawa

1994

Microbiology and Immunology

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The polypeptides of seven strains of human treponemes were investigated by immunoblot analysis for their binding to the human placental collagens and laminin. Of the treponemal polypeptides, eleven polypeptides, 45‐kDa, 49‐kDa, and 62‐kDa polypeptides from T. pallidum ATCC 27087, a 48‐kDa polypeptide from T. phagedenis biotype Reiter, 51‐kDa and 53‐kDa polypeptides from T. vincentii ATCC 35580, 30‐kDa, 53‐kDa and 63‐kDa polypeptides from T. socranskii subsp. buccale ATCC 35534, a 52‐kDa polypeptide from T. denticola ATCC 35405, and a 53‐kDa polypeptide from T. denticola ATCC 33520 possessed an ability to bind to the laminin, type I, III, IV, or V collagen. An intermediate‐sized human oral isolate strain G7201 did not possess any laminin‐ or collagen‐binding polypeptides. Immunoelectron microscopy using intact treponemal cells with a single collagen‐binding polypeptide and the corresponding antisera demonstrated that the 51‐kDa and 53‐kDa polypeptides from T. vincentii, the 53‐kDa polypeptide from T. socranskii subsp. buccale ATCC 35534 and the 52‐kDa polypeptide from T. denticola ATCC 35405, were outer envelope proteins.

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Section: Discussionmentioning

confidence: 77%

Binding of Host‐Associated Treponeme Proteins to Collagens and Laminin: A Possible Mechanism of Spirochetal Adherence to Host Tissues

Umemoto

Namikawa

1994

Microbiology and Immunology

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“…This suggested that teichoic acid specifically binds to the cells. The reversibility of teichoic acid binding to HeLa cells is plausible because that of S. aureus adherence to collagen (17) in vitro has been also reported, and to bone sialoprotein (25) and thrombospondin (16) as well as heparan sulfate (20), but not to fibronectin (24).…”

Section: Discussionmentioning

confidence: 97%

“…Staphylococcus aureus has three known adhesins, the laminin receptor (21), fibronectin receptor (13,14,22,24,25), and collagen receptor (17,26), and some putative adhesins, including teichoic acid (2,3,(6)(7)(8), lipoteichoic acid (9), protein A (11), etc. S. aureus may have other adhesins because host cells have many kinds of molecules other than the known extracellular matrices on the surface.…”

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confidence: 99%

Isolation and Characterization of Teichoic Acid‐Like Substance as an Adhesin of Staphylococcus aureus to HeLa Cells

Matsuura

Miyake

Nakashima

et al. 1996

Microbiology and Immunology

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A cell wall component that bound to HeLa cells (HeLa cell-binding CWC) was isolated from a clinical isolate of Staphylococcus aureus. The HeLa cell-binding CWC was resistant to heat (100 C, 1 hr) and proteases, did not stain with Coomassie Brilliant Blue R-250 on SDS-PAGE but stained as a broad band with antiserum against the strain on Western blots. These data suggest that the HeLa cell-binding CWC is not a protein, and may be teichoic acid. Purified teichoic acid bound to HeLa cells, whereas fractions without teichoic acid did not. In Western blots, HeLa cell-binding CWC appeared as a broad band of less than 35 kDa, similar to that of purified teichoic acid. These data suggest that the HeLa cell-binding CWC obtained in this study is teichoic acid. Teichoic acid inhibited S. aureus adherence to HeLa cells and bound to the cells time and dose dependently, in a saturable and reversible manner, and therefore appears to be an adhesin of S. aureus to HeLa cells.

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“…Previous studies have shown that bacteria may bind to fibronectin (7,15,23,25,26,32), laminin (7,16,27,29,32), and collagen (3,7,12,32) (5,23). These bacteria have been demonstrated to bind to the N-terminal region of fibronectin with high affinity (19).…”

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confidence: 99%

Binding of collagen to Staphylococcus aureus Cowan 1

Speziale¹,

Raucci²,

Visai³

et al. 1986

J Bacteriol

128

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(Pro-Gly-Pro)., (Pro-Pro-Gly)jo, and (Pro-OH-Pro-Gly)j0 were recognized by the receptor, whereas the peptides (Pro-Ala-Gly). and polyproline showed no inhibitory activity.The matrix proteins fibronectin and laminin may mediate the substrate adhesion of eucaryotic cells, and putative receptors present on the surfaces of cells are believed to recognize distinct sites in the adhesive proteins (35). Some eucaryotic cells (e.g., hepatocytes and chondrocytes) may also adhere to collagen substrate, and the presence of collagen-specific receptors has been implicated (18,22). The collagen receptor on hepatocytes appears to have broad specificity, since it binds to several different types of collagen as well as to isolated collagen a chains, collagen peptides, and synthetic collagen analogs (22).In the process of tissue adherence of pathogenic bacteria, structures at the host cell surface or in the extracellular matrix are recognized by specific receptors present on the bacterial cells. Previous studies have shown that bacteria may bind to fibronectin (7, 15, 23, 25, 26, 32), laminin (7, 16, 27, 29, 32), and collagen (3, 7, 12, 32) Chemicals. Type II collagen was purified from bovine nasal septum as described by Strawich and Nimmi (28). Native collagen types I and III were isolated with neutral salt from fetal bovine skin and purified by NaCl precipitation and DEAE chromatography (30). Type IV collagen was isolated from mouse tumor (31). Type V and VI collagens were purified from a pepsin digest of human placenta (1,20). The 1(I) and 2(I) chains both from calf and rat skin type I collagens were purified by carboxymethyl cellulose chromatography (21). The rat a chains were treated with cyanogen bromide, and the generated peptides (CB peptides) were purified as previously described (2, 6). The isolated peptides included CB2, CB5, CB6, CB7, and CB8 from the 1(I) chain and CB3, CB4, and CB5 from the a2 chain of rat type

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Specific Binding of Collagen to Staphylococcus Aureus

Cited by 55 publications

References 17 publications

Binding of Host‐Associated Treponeme Proteins to Collagens and Laminin: A Possible Mechanism of Spirochetal Adherence to Host Tissues

Binding of Host‐Associated Treponeme Proteins to Collagens and Laminin: A Possible Mechanism of Spirochetal Adherence to Host Tissues

Isolation and Characterization of Teichoic Acid‐Like Substance as an Adhesin of Staphylococcus aureus to HeLa Cells

Binding of collagen to Staphylococcus aureus Cowan 1

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