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

Abstract

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...

Is the GehD Lipase from Staphylococcus epidermidis a Collagen Binding Adhesin?

“…Almost all S. epidermidis strains are able to attach to native abiotic surfaces (3)(4)(5)(6). However, any foreign material implanted into the human body is quickly coated with various plasma proteins such as fibrinogen, fibronectin, and vitronectin (7,8), and Staphylococcus aureus, which is also a common cause of biomaterial centered infections, appears to adhere to this protein coat via adhesins of the microbial surface components recognizing adhesive matrix molecules (MSCRAMMs) 1 type.…”

Micro-scale surface-patterning influences biofilm formation

“…Some have suggested (Waldvogel and Bisno, 2000;Götz, 2002) that S. aureus requires serum proteins to attach in vivo; these conditions were not met in this work and may account for sparse biofilm compared to that formed by S. epidermidis and P. aeruginosa. However, others have found greater variability in biofilm formation by staphylococci and this variability appears to be associated with the type of serum protein and, perhaps, the nature of the substrate (Herrmann et al 1988), and the strain understudy. Even though we did not explore the influence of serum proteins on biofilm formation, it remains clear that micro-scale patterning of surfaces influenced how cells of the three strains attached to surfaces.…”

Cell surface hydrophobicity and adherence to extra–cellular matrix proteins in two collections of methicillin–resistantStaphylococcus aureus

“…Unless otherwise stated, all isolates were cultured on blood agar and grown at 37 'C for [18][19][20] [14]. Phenylsepharose CL4B gel suspensions were equilibrated with 0-01 M sodium phosphate buffer (pH [6][7][8] containing 4M sodium chloride and poured as columns in pasteur pipettes (height of column 2-0 cm, internal diameter 5 mm).…”

“…Adhesin-receptor mechanisms include binding to various components of the extracellular matrix of host tissues and adhesion of S. aureus to collagen [7], laminin [8], fibronectin [7,[9][10][11] and vitronectin [12,13] has been explored. Among nonspecific mechanisms hydrophobic interaction seems to play an important role both in the attachment of bacteria to each other and of bacteria to tissue or foreign bodies [14].…”