Binding of a Staphylococcus aureus bone pathogen to type I collagen

Microb Pathog. 1990 Jun;8(6):441-8. 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 constant, Kd = 2 x 10(-9) M). The extent of binding was similar to Cowan 1. Binding was saturable and not inhibited by 100 mM solutions of D-glucose, D-galactose, D-mannose, methyl-alpha-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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Collagen / metabolism*
  • Glycine / pharmacology
  • Humans
  • Hydroxyproline / pharmacology
  • Microscopy, Electron, Scanning
  • Monosaccharides / pharmacology
  • Osteomyelitis / microbiology
  • Rats
  • Staphylococcus aureus / metabolism*
  • Trypsin / pharmacology


  • Monosaccharides
  • Collagen
  • Trypsin
  • Hydroxyproline
  • Glycine