Specific binding of collagen type IV to Streptococcus pyogenes.
Many strains of Streptococcus pyogenes are capable of binding type IV collagen. In the present study, all 50 S. pyogenes strains isolated from patients with acute glomerulonephritis showed high or moderate affinity for radiolabelled type IV collagen. A majority of strains of other sources, such as reference strains of various M-types and strains isolated from patients with pharyngeal infections also bound type IV collagen; however, a number of weak binders or non-binders were found among those. The collagen type IV binding component(s) on S. pyogenes were susceptible to proteinase K digestion, partially sensitive to trypsin but insensitive to pepsin treatment at pH 5.5. According to tests with three M-positive strains and their M-negative derivatives, the binding was not dependent on M-protein. The binding was saturable with time and inhibited by unlabelled type IV collagen. Partially inhibition was found with type II collagen, gelatin and fibrinogen but not with a number of other serum proteins.
Kostrzynska
M
M
National Institute of Hygiene, Department of Bacteriology, Warsaw, Poland.
Schalén
C
C
Wadström
T
T
D003094:Collagen / Q000378:metabolism*; D005921:Glomerulonephritis / Q000209:etiology; D006801:Humans; D013297:Streptococcus pyogenes / Q000378:metabolism* / Q000472:pathogenicity
D003094:Collagen