Binding of a Staphylococcus aureus bone pathogen to type I collagen

• Published in: Microbial pathogenesis Vol. 8; no. 6; pp. 441 - 448
• Main Authors: Buxton, Thomas B., Rissing, J.Peter, Horner, Jack A., Plowman, Kent M., Scott, David F., Sprinkle, Terry J., Best, Gary K.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier India Pvt Ltd 01.06.1990; Elsevier
• Subjects: Animals; Bacteriology; Biological and medical sciences; collagen; Collagen - metabolism; collagen-binding; Fundamental and applied biological sciences. Psychology; Glycine - pharmacology; Humans; Hydroxyproline - pharmacology; l-fucose; Microbiology; Microscopy, Electron, Scanning; Monosaccharides - pharmacology; osteomyelitis; Osteomyelitis - microbiology; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Rats; Staphylococcus aureus; Staphylococcus aureus - metabolism; Trypsin - pharmacology; osteomyelitis; collagen; collagen-binding; l-fucose; Staphylococcus aureus; Radiolabelling; Diseases of the osteoarticular system; Molecular interaction; Adhesion; Strain; Infection; Microorganism capsule; Pathogenicity; Collagen; Bacteriosis; Lipopolysaccharide; Bacteria; Micrococcales; Micrococcaceae; Bone; Fucose
• ISSN: 0882-4010; 1096-1208
• DOI: 10.1016/0882-4010(90)90031-K

We contrasted the collagen-binding potential of the experimental osteomyelitis pathogen, Staphylococcus aureus strain SMH, to several other strains. These included Cowan 1 (binder), Wood 46 (non-binder) and six capsular variants. These measurements were made using an 125I-collagen binding assay. Formalin-killed S. aureus SMH strongly bound commercial type I iodinated collagen (dissociation contant, K d = 2 × 10 −9 m). The extent of binding was similar to Cowan 1. Binding was saturable and not inhibited by 100 m m solutions of d-glucose, d-galactose, d-mannose, methyl-α- l-fucopyranoside, l-hydroxyproline or l-glycine. d-lactose gave moderate inhibition of binding to collagen, and l-fucose was strongly inhibitory. Trypsinized SMH did not bind collagen. None of four Ruthenium-red-staining staphylococci (encapsulated) avidly bound type I collagen. The encapsulated Smith strain, for example, did not bind to collagen but its capsule-negative variant, Smith compact, showed extensive binding. Three of five non-encapsulated S. aureus were strong collagen binders. These data suggest that the prototype bone pathogen binds to the major protein component of bone's extracellular matrix. Collagen-binding is promoted by protein adhesin(s), not capsule. The latter, in fact, appeared to interfere with this interaction. Binding was inhibited by solutions containing the simple monosaccharide, l-fucose.