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Anti–factor H autoantibodies block C-terminal recognition function of factor H in hemolytic uremic syndrome

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TLDR
It is suggested that aHUS-associated FH autoantibodies mimic the effect of C-terminal FH mutations, as they inhibit the regulatory function of FH at cell surfaces by blocking its C-Terminal recognition region.
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This article is published in Blood.The article was published on 2007-09-01 and is currently open access. It has received 239 citations till now. The article focuses on the topics: Atypical hemolytic uremic syndrome & Factor H.

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Journal ArticleDOI

Atypical Hemolytic–Uremic Syndrome

TL;DR: Current concepts about the pathobiology of atypical hemolytic–uremic syndrome are reviewed and its diagnosis and management are reviewed.
Journal Article

[Hemolytic-uremic syndrome].

Cutillo S
- 30 Jun 1973 - 
Journal ArticleDOI

Atypical hemolytic uremic syndrome

TL;DR: Case reports and two phase II trials show an impressive efficacy of the complement C5 blocker eculizumab, suggesting it will be the next standard of care.
Journal ArticleDOI

Factor H autoantibodies in atypical hemolytic uremic syndrome correlate with CFHR1/CFHR3 deficiency

TL;DR: A novel subgroup of aHUS is defined, termed DEAP HUS (deficiency of CFHR proteins and CFH autoantibody positive) that is characterized by a combination of genetic and acquired factors.
Journal ArticleDOI

STEC-HUS, atypical HUS and TTP are all diseases of complement activation

TL;DR: Evidence is emerging that pharmacological targeting of complement with the anti-C5 monoclonal antibody eculizumab can effectively treat not only aHUS for which it is indicated, but also STEC-HUS and TTP in some circumstances.
References
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Journal Article

[Hemolytic-uremic syndrome].

Cutillo S
- 30 Jun 1973 - 
Journal ArticleDOI

Hemolytic Uremic Syndrome

TL;DR: In this paper, a review summarizes current concepts about the epidemiological findings, the pathological and clinical aspects of STEC-HUS, pneumococcal HUS, and aHUS and their diagnosis and management.
Journal ArticleDOI

Anti–Factor H Autoantibodies Associated with Atypical Hemolytic Uremic Syndrome

TL;DR: It is supported for the first time that HUS may occur in a context of an autoimmune disease with the development of anti-FH-specific antibody leading to an acquired FH deficiency, which may lead to the design of new approaches of diagnosis and treatment in plasma exchanges or immunosuppressive therapies.
Journal ArticleDOI

Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome

TL;DR: In this article, three mutations (E1172Stop, R1210C, and R1215G) were identified in the C-terminal region of the complement regulator factor H and each of the three mutations caused reduced binding to the central complement component C3b/C3d.
Journal ArticleDOI

Structural and functional characterization of factor H mutations associated with atypical hemolytic uremic syndrome

TL;DR: The hypothesis that patients with aHUS carry a specific dysfunction in the protection of cellular surfaces from complement activation is supported, offering new possibilities to improve diagnosis and develop appropriate therapies.
Related Papers (5)
Frequently Asked Questions (15)
Q1. What contributions have the authors mentioned in the paper "Anti-factor h autoantibodies block c-terminal recognition function of factor h in hemolytic uremic syndrome" ?

Józsi et al. this paper described how five FH-autoantibodies affect FH function. 

Mutations identified in complement genes in aHUS patients indicate that complement dysregulation is involved in disease development. 

(B) Autoantibody binding to FH was blocked with mAbs (25 µg/ml) specific to the C-terminal domains SCR19-20 of FH, i.e. C02, C14 and C18, whereas mAbs N11, M12, M13 and M15, which bind in the N-terminal and middle regions of FH, did not inhibit autoantibody binding. 

FH-autoantibodies of aHUS patients bind to the C-terminus of FH Plasma samples from 60 patients with hemolytic uremic syndrome (51 with aHUS and 9 with D+ HUS) were screened for the presence of FH-autoantibodies. 

4Hemolysis assays were performed in 100 µl buffer (20 mM HEPES, 7 mM MgCl2, 10 mM EGTA, 144 mM NaCl, 1% BSA, pH 7.4) containing 5×106 sheep erythrocytes (SRBC,BioTrend Chemikalien GmbH, Cologne, Germany) and 10-40% plasma. 

HUS is most often caused by bacterial infection and is associated with diarrhea (D+ HUS), or arises rarely as atypical HUS (aHUS). 

FH-autoantibody inhibits C-terminus mediated function of FH Reduced C3b binding of FH and impaired C3b processing on the cell surface, which results in enhanced complement activation and cell damage, is caused by the mAbs C18 and C14,11 which share binding epitopes with the autoantibodies of all five analyzed aHUS patients (Figure 1C). 

(B) Dose-dependent binding of the autoantibody positive plasma samples of five aHUS patients to immobilized FH, indicating different autoantibody titers. 

the hemolytic activity was reversed in a dose-dependent manner by addition of excess FH to the patient’s plasma, and thus increasing the concentration of autoantibody-free FH (Figure 2C). 

C3b binding was strongly reduced when FH was preincubated with patient derived IgG, which contained FH-autoantibodies, whereas control IgG had no effect (Figure 2A). 

(A) Plasma samples of aHUS (n = 51) and D+ HUS (n = 9) patients as well as healthy donors (n = 30) were analyzed for binding on immobilized purified FH in an ELISA assay. 

for the autoantibody positive patients kidney transplant is likely at high risk, as the autoreactive antibodies will remain in plasma. 

In addition, factor H (FH)-autoantibodies have been reported for three aHUS-patients.3FH is a major regulator of the alternative complement pathway. 

6,11 In all five cases, binding of the autoantibody to FH was reduced by mAbs which bind to the FH C-terminus, namely mAbs C02 (binding in SCR19), C14 and C18 (both binding within SCR20). 

This effect of the autoantibody is in line with the observation, that the C-terminally binding mAbs C18 and C14 cause enhanced SRBC lysis when added to normal human plasma (data not shown).