Binding of a Staphylococcus aureus bone pathogen to type I collagen.
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.
Buxton
T B
TB
Veterans Administration Medical Center, Augusta, GA 30910.
Rissing
J P
JP
Horner
J A
JA
Plowman
K M
KM
Scott
D F
DF
Sprinkle
T J
TJ
Best
G K
GK
D000818:Animals; D003094:Collagen / Q000378:metabolism*; D005998:Glycine / Q000494:pharmacology; D006801:Humans; D006909:Hydroxyproline / Q000494:pharmacology; D008855:Microscopy, Electron, Scanning; D009005:Monosaccharides / Q000494:pharmacology; D010019:Osteomyelitis / Q000382:microbiology; D051381:Rats; D013211:Staphylococcus aureus / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology
D009005:Monosaccharides; D003094:Collagen; D014357:Trypsin; D006909:Hydroxyproline; D005998:Glycine