Variations in binding of mammalian fibrinogens to streptococci groups A, B, C, E, G and to Staphylococcus aureus.
Twenty-eight beta-hemolytic streptococci of groups A, B, E, G and Streptococcus equisimilis as well as four Staphylococcus aureus strains were tested for their ability to bind fibrinogen preparations from different animal species: homo, baboon, rabbit, rat, guinea-pig, dog, horse, pig, cow and sheep. The patterns of binding indicated differences in the structures of the bacterial fibrinogen receptors. There were higher binding levels in streptococci groups A, G, and S. equisimilis than in representative group B and E strains. Considerable differences in the binding capacity were found within streptococci groups A and E. Group C and group G strains showed rather similar patterns and could be further divided into high-level and low-level binding strains. There is no correlation between binding levels of different animal fibrinogen preparations and the strains isolated from corresponding animals. Recent studies by others have shown that resistance to phagocytosis is mediated by fibrinogen-binding in streptococci group A. The existence of similar fibrinogen-binding structures in several streptococcal species indicates an important role with a definite survival value. It also suggests that M or T protein analogues are present in streptococci groups C, G and E.
Reuterswärd
A
A
Miörner
H
H
Wagner
M
M
Kronvall
G
G
D000818:Animals; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D010980:Platelet Membrane Glycoproteins; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013045:Species Specificity; D013211:Staphylococcus aureus / Q000378:metabolism*; D013291:Streptococcus / Q000378:metabolism*
D010980:Platelet Membrane Glycoproteins; D011956:Receptors, Cell Surface; D005340:Fibrinogen