Plasma Concentrations of Complement-Modulating Proteins (C1 Inhibitor, C4 Binding Protein, Factor H and Factor I) in Inflammatory Dermatoses with Special Reference to Psoriasis

Dermatology ◽  
1989 ◽  
Vol 179 (1) ◽  
pp. 30-34 ◽  
Author(s):  
K. Ohkohchi ◽  
W. Torinuki ◽  
H. Tagami
Keyword(s):  
Special Reference ◽  
Binding Protein ◽  
Plasma Concentrations ◽  
Factor H ◽  
C1 Inhibitor ◽  
Factor I ◽  
Protein Factor ◽  
Inflammatory Dermatoses

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 Bactericidal Antibody Responses Induced by Meningococcal Recombinant Chimeric Factor H-Binding Protein Vaccines

2008 ◽  
Vol 76 (6) ◽  
pp. 2568-2575 ◽  
Author(s):  
Peter T. Beernink ◽  
Dan M. Granoff
Keyword(s):  
Bactericidal Activity ◽  
Vaccine Candidate ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Factor H ◽  
Enzyme Linked Immunosorbent Assay ◽  
Meningococcal Vaccine ◽  
Serum Antibodies ◽  
Classical Complement Pathway ◽  
Protein Factor

ABSTRACT Factor H-binding protein (fHbp) is a novel meningococcal vaccine candidate that elicits serum antibodies that activate classical complement pathway bacteriolysis and also inhibit binding of the complement down-regulatory protein, factor H, to the bacterial surface. One limitation of fHbp as a vaccine candidate is antigenic variability, since antibodies to fHbp in the variant 1 (v.1) antigenic group do not protect against strains expressing v.2 or v.3 proteins, and vice versa. We have identified amino acid residues of epitopes recognized by bactericidal anti-fHbp monoclonal antibodies prepared against fHbp from each of the variant groups. One epitope expressed by nearly all v.1 proteins mapped to the B domain, while epitopes expressed by fHbp v.2 or v.3 mapped to the C domain. The results provided the rationale for engineering chimeric fHbp molecules containing the A domain (which is conserved across all variant groups), a portion of the B domain of a v.1 protein, and the carboxyl-terminal portion of the B domain and the C domain of a v.2 protein. By enzyme-linked immunosorbent assay, the resulting recombinant chimeric proteins expressed epitopes from all three variant groups. In mice, the chimeric vaccines elicited serum antibodies with bactericidal activity against a panel of genetically diverse strains expressing fHbp v.1, v.2, or v.3. The data demonstrate the feasibility of preparing a meningococcal vaccine from a single recombinant protein that elicits broad bactericidal activity, including group B strains, which account for 50 percent of cases of meningococcal disease and for which there currently is no broadly protective vaccine.

Human factor H and C4b-binding protein serve as factor I-cofactors both encompassing inactivation of C3b and C4b

1995 ◽  
Vol 32 (5) ◽  
pp. 355-360 ◽  
Author(s):  
Tsukasa Seya ◽  
Kimiyo Nakamura ◽  
Takahisa Masaki ◽  
Chikako Ichihara-Itoh ◽  
Misako Matsumoto ◽  
...  
Keyword(s):  
Human Factor ◽  
Binding Protein ◽  
Factor H ◽  
Factor I

scholarly journals Acquisition of Complement Inhibitor Serine Protease Factor I and Its Cofactors C4b-Binding Protein and Factor H by Prevotella intermedia

PLoS ONE ◽  
2012 ◽  
Vol 7 (4) ◽  
pp. e34852 ◽  
Author(s):  
Sven Malm ◽  
Monika Jusko ◽  
Sigrun Eick ◽  
Jan Potempa ◽  
Kristian Riesbeck ◽  
...  
Keyword(s):  
Serine Protease ◽  
Binding Protein ◽  
Factor H ◽  
Prevotella Intermedia ◽  
Complement Inhibitor ◽  
Factor I

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.

scholarly journals Functional Comparison of the Binding of Factor H Short Consensus Repeat 6 (SCR 6) to Factor H Binding Protein from Neisseria meningitidis and the Binding of Factor H SCR 18 to 20 to Neisseria gonorrhoeae Porin

2009 ◽  
Vol 77 (5) ◽  
pp. 2094-2103 ◽  
Author(s):  
Jutamas Shaughnessy ◽  
Lisa A. Lewis ◽  
Hanna Jarva ◽  
Sanjay Ram
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Neisseria Meningitidis ◽  
Binding Protein ◽  
Alternative Pathway ◽  
Factor H ◽  
Site Directed Mutagenesis ◽  
Chimeric Proteins ◽  
Inhibitory Protein ◽  
Protein Factor ◽  
Short Consensus Repeat

ABSTRACT Both Neisseria meningitidis and Neisseria gonorrhoeae recruit the alternative pathway complement inhibitory protein factor H (fH) to their surfaces to evade complement-dependent killing. Meningococci bind fH via fH binding protein (fHbp), a surface-exposed lipoprotein that is subdivided into three variant families based on one classification scheme. Chimeric proteins that comprise contiguous domains of fH fused to murine Fc were used to localize the binding site for all three fHbp variants on fH to short consensus repeat 6 (SCR 6). As expected, fH-like protein 1 (FHL-1), which contains fH SCR 6, also bound to fHbp-expressing meningococci. Using site-directed mutagenesis, we identified histidine 337 and histidine 371 in SCR 6 as important for binding to fHbp. These findings may provide the molecular basis for recent observations that demonstrated human-specific fH binding to meningococci. Differences in the interactions of fHbp variants with SCR 6 were evident. Gonococci bind fH via their porin (Por) molecules (PorB.1A or PorB.1B); sialylation of lipooligosaccharide enhances fH binding. Both sialylated PorB.1B- and (unsialylated) PorB.1A-bearing gonococci bind fH through SCR 18 to 20; PorB.1A can also bind SCR 6, but only weakly, as evidenced by a low level of binding of FHL-1 relative to that of fH. Using isogenic strains expressing either meningococcal fHbp or gonococcal PorB.1B, we discovered that strains expressing gonococcal PorB.1B in the presence of sialylated lipooligosaccharide bound more fH, more effectively limited C3 deposition, and were more serum resistant than their isogenic counterparts expressing fHbp. Differences in fH binding to these two related pathogens may be important for modulating their individual responses to host immune attack.

Interaction of C4b-binding protein, factor H and C1q with different ligands on dying cells

2008 ◽  
Vol 45 (16) ◽  
pp. 4138
Author(s):  
Myriam Martin ◽  
Jonatan Leffler ◽  
Anna M. Blom
Keyword(s):  
Binding Protein ◽  
Factor H ◽  
Protein Factor ◽  
Dying Cells

Effects of zinc on factor I cofactor activity of C4b-binding protein and factor H

2003 ◽  
Vol 418 (2) ◽  
pp. 108-118 ◽  
Author(s):  
Anna M Blom ◽  
Lena Kask ◽  
Bala Ramesh ◽  
Andreas Hillarp
Keyword(s):  
Binding Protein ◽  
Factor H ◽  
Factor I ◽  
Cofactor Activity
Sign in / Sign up

Export Citation Format

Share Document