Fibrinogen and Fibrin Degradation Products and the Clumping of Staphylococci by Serum

Allington, M. J.

doi:10.1111/j.1365-2141.1967.tb00763.x

Cited by 67 publications

(15 citation statements)

References 13 publications

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“…aureus binds specifically to soluble fibrinogen in a reaction described as staphylococcal clumping reaction [43,44] and to surface-bound fibrinogen [35], possibly via a recently described receptor protein [45]. Our observation of the extent of increased adherence of S. aureus to foreign surfaces because of fibrinogen therefore suggests a contribution of this protein to colonization and infection of catheters with S. aureus.…”

Section: Herrmann Et Afmentioning

confidence: 76%

Fibronectin, Fibrinogen, and Laminin Act as Mediators of Adherence of Clinical Staphylococcal Isolates to Foreign Material

Herrmann

Vaudaux²,

Pittet³

et al. 1988

The Journal of Infectious Diseases

494

269

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Bacterial adherence to polymer surfaces is a required early step in intravenous (iv) device infection. Wecollected eight strains of Staphylococcus aureus and 19of coagulase-negative staphylococci from patients with proven iv device bacteremia and studied the role of plasma or connective-tissue proteins in promoting bacterial adherence to polymethylmethacrylate (PMMA) coverslips. Although only a negligible percentage of organisms adhered to albumin-coated PMMA, surface-bound fibronectin significantly promoted adherence of all isolates. Fibrinogen markedly promoted adherence of all S. aureus strains but of only four coagulase-negative strains. Thus, coagulase-negative staphylococci revealed a marked heterogeneity in adherence to fibrinogen-coated surfaces, a result suggesting the existence of heretofore unknown receptors for fibrinogen. Laminin promoted adherence of staphylococci to a much lower extent. Although strain specific, adherence of clinical staphylococcal isolates to foreign surfaces is significantly increased by fibronectin, fibrinogen, and laminin, an observation suggesting the possible contribution of these proteins to the pathogenesis of iv device infection.Adherence of microorganisms to specific substrates is presently considered to be a crucial step in the initiation of infections [1]. Many investigators have searched for such ligands in staphylococcal prosthesis infection. There is increasing evidence that similar specific interactions might also playa role in the pathogenesis of foreign-body infections.After contact with blood, a polymer surface (such as a cannula inserted iv) is almost immediately coated with a protein layer at the blood-polymer interface [2][3][4]. Bacterial adherence to the protein-coated surface is a prerequisite for initiating iv device infection. Fibrinogen and fibronectin are proteins known to bind and to aggregate staphylococci [5,6]. More recently, laminin, a large glycoprotein mainly found Receivedfor publication 2 December 1987and in revised form 7 April 1988. This paper was presented in part at the 27th Interscience Conference on Antimicrobial Agents and Chemotherapy (abstract 503), held on 4-7 October 1987, in New York, New York.This work was supported by grant 3.829-0.87 from the Swiss National Research Foundation.We thank Elzbieta Huggler for technical assistance, Dr. Ingeborg Filthuth and Chantal Genier for isolation and characterization of the bacterial isolates, and Paule Schilling-Doriot for manuscript preparation.Please address requests for reprints to Dr. Mathias Herrmann, Infectious Diseases Division, Department of Medicine, University Hospital, CH-1211 Geneva 4, Switzerland. 693in basal membranes and to a slight extent in plasma, has also been described as possessing staphylococcalbinding properties [7]. Several studies have investigated staphylococcal adherence [8][9][10][11] to polymer surfaces. In particular, studies performed on explanted foreign bodies [12,13]and on in vitro models [14,15]strongly suggested that adherence of selected staphylococcal str...

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Section: Herrmann Et Afmentioning

confidence: 76%

Fibronectin, Fibrinogen, and Laminin Act as Mediators of Adherence of Clinical Staphylococcal Isolates to Foreign Material

Herrmann

Vaudaux²,

Pittet³

et al. 1988

The Journal of Infectious Diseases

494

269

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“…Controls using human platelets in identical media gave the expected results. Fibrinogen was assayed by the staphylococcal clumping test [2] using the Sigma kit and human fibrinogen as a standard. The immunodiffusion plate system (M-PartigenFibrinogen, Behring) was used to confirm the results of the clumping assay.…”

Section: Marker Assaysmentioning

confidence: 99%

Isolation and partial characterization of platelet α-granule membranes

1983

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Porcine alpha-granules, prepared by a modification of pre-existing methods, were found to be essentially homogeneous by transmission electron microscopy. Freeze-fractured samples of isolated granules revealed numerous intramembranous particles on the EF (exoplasmic fracture) surface and to a lesser extent on the PF (protoplasmic fracture) surface whereas the PS (protoplasmic) surface was relatively smooth. The granules appear to be sealed, as evidenced by: a) the retention of their electron dense core material; b) the inability of impermeant labels to react with the granule contents, and c) the finding that the intragranular proteins are refractory to mild hydrolysis by externally added proteases. Membranes were isolated by alkali extraction of the granules and used for biochemical characterization. Approximately 87% of the protein, but only insignificant amounts of phospholipid were removed by this procedure, which yielded membrane vesicles devoid of the dense core. The membranes contain one major and several minor polypeptides of molecular weights ranging from 28,000 to 230,000, as determined by polyacrylamide gel electrophoresis. The major polypeptide contains carbohydrate residues. The exposure of specific proteins on the cytoplasmic surface of the granule membrane was determined by a combination of surface-specific labeling and proteolysis of intact granules, followed by membrane isolation and analysis. In sealed granules, only a limited number of bands are modified by the reagents whereas most of them are affected following granule lysis, indicating asymmetry in their transmembrane disposition. The fraction eluted by alkali extraction was also analyzed and found to contain nine major polypeptides of molecular weights ranging from 230,000 to 43,000. These are compared to the weights of the macromolecules believed to be secreted from alpha-granules, as determined by radioimmunological techniques.

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“…The capsule, mainly composed of acidic polysac charides, is present in less than 50% of the strains of Staphylococcus aureus and inhibits phagocytosis by interfering with opsonization [29], The clumping fac tor reacts with fibrinogen or with soluble fibrin mon omer complexes causing the clumping of staphylo cocci in the presence of plasma, a phenomenon that may also interfere with phagocytosis [30,31]. Protein A shows biological activity on coagulation, on nonspecific defense and immune reactions.…”

Section: Staphylococcal Cell Wall Componentsmentioning

confidence: 99%