Monoclonal antibodies against the complement control protein Factor H (β1 H)

1983 ◽  
Vol 3 (12) ◽  
pp. 1119-1131 ◽  
Author(s):  
E. Sim ◽  
M. S. Palmer ◽  
M. Puklavec ◽  
R. B. Sim
Keyword(s):  
Monoclonal Antibodies ◽  
Human Factor ◽  
Factor H ◽  
Single Chain ◽  
Chain Molecules ◽  
Complement Control Protein ◽  
Protein Factor ◽  
Green Monkey ◽  
Cofactor Activity ◽  
Control Protein

Two mouse monoclonal antibodies against the human complement control protein, Factor H (β1H), are described. The antibodies are both IgG − γ1 - subclasses and are directed against different epitopes on the human Factor H molecule. One of the antibodies, MRC OX 24, increases the cofactor activity of Factor H in Factor I-mediated cleavage of soluble C3b. The second antibody, MRC OX 23, which has no effect alone, reduces the increase in cofactor activity observed in the presence of the first antibody. However, MRC OX 24 inhibits the binding of 125I-labelled Factor H to surface-bound C3b (EAC3b). Again MRC OX 23 alone does not have any effect but decreases the inhibition in 125I-Labelled Factor H binding to EAC3b observed with MRC OX 24. These studies show clearly that the interaction of Factor H with soluble C3b is different to its interaction with surface-bound C3b. In an indirect immunoprecipitation system using these monoclonal antibodies, single-chain molecules of 150 000 mol. wt. are specifically precipitated from human serum and also from the sera of other primates - rhesus monkey, cynomolgus monkey, and African green monkey. There was no precipitation from sera of cow, pig, sheep, chick, or rabbit. Using a radioimmunoassay with radiolabelled monoclonal MRC OX 23, the concentration of Factor H in human plasma was determined.

scholarly journals SP105ATYPICAL HEMOLYTIC UREMIC SYNDROME AND C3 GLOMERULOPATHY DUE TO MONOCLONAL ANTIBODY AGAINST COMPLEMENT CONTROL PROTEIN FACTOR H

2019 ◽  
Vol 34 (Supplement_1) ◽  
Author(s):  
Paraskevi Eva Andronikidis ◽  
Papanikolaou Vasiliki ◽  
Plavoukou Styliani ◽  
Tsouka Glykeria ◽  
Delibasi Sosanna ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Hemolytic Uremic Syndrome ◽  
Factor H ◽  
C3 Glomerulopathy ◽  
Complement Control Protein ◽  
Protein Factor ◽  
Uremic Syndrome ◽  
Control Protein

scholarly journals Complement control protein factor H: The good, the bad, and the inadequate

2010 ◽  
Vol 47 (13) ◽  
pp. 2187-2197 ◽  
Author(s):  
Viviana P. Ferreira ◽  
Michael K. Pangburn ◽  
Claudio Cortés
Keyword(s):  
Factor H ◽  
Complement Control Protein ◽  
Protein Factor ◽  
Control Protein

Functional properties of the allotypes of mouse complement regulatory protein, factor H: Difference of compatibility of each allotype with human factor I

1993 ◽  
Vol 30 (9) ◽  
pp. 841-848 ◽  
Author(s):  
Okada Michiyo ◽  
Kojima Ayako ◽  
Takano Hiromi ◽  
Harada Yoshinobu ◽  
Nonaka Mayumi ◽  
...  
Keyword(s):  
Functional Properties ◽  
Human Factor ◽  
Regulatory Protein ◽  
Factor H ◽  
Complement Regulatory Protein ◽  
Factor I ◽  
Protein Factor

scholarly journals Human Factor H-Related Protein 5 Has Cofactor Activity, Inhibits C3 Convertase Activity, Binds Heparin and C-Reactive Protein, and Associates with Lipoprotein

2005 ◽  
Vol 174 (10) ◽  
pp. 6250-6256 ◽  
Author(s):  
Jennifer L. McRae ◽  
Thomas G. Duthy ◽  
Kim M. Griggs ◽  
Rebecca J. Ormsby ◽  
Peter J. Cowan ◽  
...  
Keyword(s):  
Human Factor ◽  
Factor H ◽  
Related Protein ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Cofactor Activity

Solution structure of the fifth repeat of factor H: a second example of the complement control protein module

Biochemistry ◽  
1992 ◽  
Vol 31 (14) ◽  
pp. 3626-3634 ◽  
Author(s):  
P. N. Barlow ◽  
D. G. Norman ◽  
A. Steinkasserer ◽  
T. J. Horne ◽  
J. Pearce ◽  
...  
Keyword(s):  
Solution Structure ◽  
Factor H ◽  
Complement Control Protein ◽  
Control Protein

scholarly journals Clumping Factor A Interaction with Complement Factor I Increases C3b Cleavage on the Bacterial Surface of Staphylococcus aureus and Decreases Complement-Mediated Phagocytosis

2010 ◽  
Vol 78 (4) ◽  
pp. 1717-1727 ◽  
Author(s):  
Pamela S. Hair ◽  
Charlene G. Echague ◽  
Amber M. Sholl ◽  
Justin A. Watkins ◽  
Joan A. Geoghegan ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Surface Protein ◽  
Factor H ◽  
Complement Factor ◽  
Wild Type ◽  
Bacterial Surface ◽  
Complement Control Protein ◽  
Factor I ◽  
Protein Factor ◽  
Fibrinogen Binding

ABSTRACT The human complement system is important in the immunological control of Staphylococcus aureus infection. We showed previously that S. aureus surface protein clumping factor A (ClfA), when expressed in recombinant form, bound complement control protein factor I and increased factor I cleavage of C3b to iC3b. In the present study, we show that, compared to the results for the wild type, when isogenic ClfA-deficient S. aureus mutants were incubated in serum, they bound less factor I, generated less iC3b on the bacterial surface, and bound fewer C3 fragments. It has been shown previously that two amino acids in ClfA (P336 and Y338) are essential for fibrinogen binding. However, S. aureus expressing ClfA(P336A Y338S) was less virulent than ClfA-deficient strains in animal models. This suggested that ClfA contributed to S. aureus virulence by a mechanism different than fibrinogen binding. In the present study, we showed that S. aureus expressing ClfA(P336A Y338S) was more susceptible to complement-mediated phagocytosis than a ClfA-null mutant or the wild type. Unlike ClfA, ClfA(P336A Y338S) did not enhance factor I cleavage of C3b to iC3b and inhibited the cofactor function of factor H. Fibrinogen enhanced factor I binding to ClfA and the S. aureus surface. Twenty clinical S. aureus strains all expressed ClfA and bound factor I. High levels of factor I binding by clinical strains correlated with poor phagocytosis. In summary, our results suggest that the interaction of ClfA with factor I contributes to S. aureus virulence by a complement-mediated mechanism.

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