Binding of complement subcomponent C1q to Streptococcus pyogenes: evidence for interactions with the M5 and FcRA76 proteins

• Published in: FEMS immunology and medical microbiology 1998, Vol.20 (1), p.11-20
• Main Authors: Koroleva, Irina V, Sjöholm, Anders G, Schalén, Claes
• Format: Article
• Language: English
• Subjects: Antigens, Bacterial; Bacterial Outer Membrane Proteins; Bacterial Proteins - metabolism; Binding Sites; Blotting, Western; C1q; Carrier Proteins - metabolism; Complement; Complement C1q - immunology; Complement C1q - metabolism; Electrophoresis, Polyacrylamide Gel; Fibrinogen - pharmacology; Humans; Pepsin A - pharmacology; Protein Binding; Streptococcus pyogenes; Streptococcus pyogenes - immunology; Streptococcus pyogenes - metabolism; Trypsin - pharmacology
• ISSN: 0928-8244; 1574-695X
• DOI: 10.1016/S0928-8244(97)00101-6

Binding of C1q, the first component of the complement system, to some human pathogens has been earlier reported. In the present study, direct binding of C1q to group A streptococci (GAS) of various serotypes as well as some other Gram-positive and Gram-negative species was demonstrated. The interaction between C1q and GAS was investigated more in detail. In hot neutral extracts of a number of GAS strains two components of 64 and 52 kDa, respectively, bound C1q; alkaline and SDS extracts yielded the 52 kDa component as the main C1q-binding substance. Trypsin treatment of the SDS extracts of two GAS strains suggested the C1q-binding component(s) to be of protein nature. C1q-binding material purified from the SDS extract of an avirulent strain, type T27, was separated in 12% SDS-PAGE and probed in Western blot with human C1q and fibrinogen, conjugated to horse radish peroxidase (HRP) as well as rabbit IgG antibodies complexed to HRP (PAP system). The 52 kDa component was non-reactive with fibrinogen or rabbit IgG. However, C1q-binding components purified from the alkaline extracts of two M-positive strains revealed strong binding of either fibrinogen (type M5) or both fibrinogen and rabbit IgG (type M76); the molecular mass of these components, 55 kDa and 43–40 kDa, respectively, was in agreement with the reported molecular mass of the M5 and FcRA76 proteins. Our findings suggest that C1q may interact with GAS through certain M-family proteins as well as by a so far unidentified surface factor of protein nature occurring in most GAS strains. The involvement of M-family proteins, regarded as virulence factors of these organisms, may suggest the interaction of GAS with C1q as biologically important.