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Institut für Hygiene, University of Innsbruck, Innsbruck, Austria
To allow for a better characterization of the ligand binding
structures of human complement receptor type 2 (CR2; CD21), we have
established an IgG1 
mouse mAb, FE8, that interferes efficiently
with binding of C3dg and EBV to CR2. In contrast to mAb OKB7, the only
well-characterized mAb with similar specificity, mAb FE8 blocked
binding of soluble C3dg or particles carrying multiple copies of
surface-bound C3dg to CR2 or induced complete removal of these ligands
from the receptor. In vitro EBV infection of B lymphocytes, on the
other hand, was abrogated by mAbs FE8 and OKB7 with similar
dose-response characteristics. As FE8 was shown to recognize a
discontinuous epitope, a series of overlapping peptides derived from
SCR1 and -2 and immobilized on cellulose was screened with FE8. The
results suggest that up to five discontinuous sequences contributed to
the epitope. The sequence 63-EYFNKYS-69, located between the two SCR
units, reacted most intensively. Two other sequences, 16-YYSTPI-21 and
105-NGNKSVWCQANN-116, are located between Cys1 and
Cys2 of SCR1 and around Cys3 of SCR2,
respectively. Based on the solution structure for two factor H SCRs, a
three-dimensional model of SCR1 and -2 was generated. The FE8 binding
peptide sequences were located in relative proximity to each other,
bounding the recess formed between SCR1 and -2. This potential of mAb
FE8 is currently unique and may be exploited for interfering with
conditions of unwanted recognition of C3dg-coated structures by the
immune system.
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