Functional Characterization of the Disease-Associated N-Terminal Complement Factor H Mutation W198R.

ABSTRACT: Dysregulation of the complement alternative pathway is involved in the pathogenesis of several diseases, including the kidney diseases atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathy (C3G). In a patient, initially diagnosed with chronic glomerulonephritis, possibly C3G, and who 6 years later had an episode of aHUS, a heterozygous missense mutation leading to a tryptophan to arginine exchange (W198R) in the factor H (FH) complement control protein (CCP) 3 domain has previously been identified. The aim of this study was to clarify the functional relevance of this mutation. To this end, wild-type (FH1-4_WT) and mutant (FH1-4_W198R) CCPs 1-4 of FH were expressed as recombinant proteins. The FH1-4_W198R mutant showed decreased C3b binding compared w

SUBMITTER: Cserhalmi M 

PROVIDER: S-EPMC5733548 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature