Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome
J. Clin. Invest. Tamara Manuelian, et al. 111:1181 doi:10.1172/JCI16651 [Go to this article.]

Figure 6
Binding of recombinant wild-type and mutant factor H proteins to HUVECs: immunofluorescence. HUVECs cultivated in serum-free medium were incubated with cell culture supernatant containing the indicated recombinant proteins, i.e., the recombinant wild-type protein (FH 8-20; WT) (a), the R1210C mutant (i.e., FH 8-20/R1210C) (b), and the R1215G mutant (i.e., FH 8-20/R1215G) (c), and FH 8-11 (d) was used as a control. Unfixed cells were used directly for immunofluorescence analysis by staining with factor H antiserum in combination with an FITC-labeled secondary antiserum. The bars in the lower corner show the length of 20 μm.