Analysis of the recognition mechanism of the alternative pathway of complement by monoclonal anti-factor H antibodies: evidence for multiple interactions between H and surface bound C3b.
FEBS Lett
; 393(2-3): 297-302, 1996 Sep 16.
Article
en En
| MEDLINE
| ID: mdl-8814308
ABSTRACT
The ability of the alternative pathway of complement to discriminate targets as either activators or non-activators is mediated by different binding properties of factor H to surface-associated C3b molecules. In the present study we have probed the interaction between H and C3b using five anti-H mAb. The binding sites of the mAb were mapped by Western blotting using both recombinant and trypsin-generated H fragments. Two mAb bound to CCP1 (90X, 196X), two to CCP5 (MRC OX24, 86X) and one to CCP8-15a (131X). At a molar ratio 21 of 125I-HmAb all tested mAb enhanced binding of H to both activator- and non-activator-bound C3b. At higher concentrations two mAb had an inhibitory effect on H binding to surface-associated C3b (OX24, 131X). Thus the mAb 131X inhibits H binding to surface-bound C3b but unlike OX24 it does not bind to the previously described C3b binding site within or near CCP4-5. These results indicate that there is an additional interaction site on factor H for surface-bound C3b.
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Banco de datos:
MEDLINE
Asunto principal:
Complemento C3b
/
Factor H de Complemento
/
Vía Alternativa del Complemento
Límite:
Animals
/
Humans
Idioma:
En
Año:
1996
Tipo del documento:
Article