Abstract:
:To identify the linear epitope for Fc-binding on the bovine IgG2 Fc receptor (boFcgamma2R), peptides derived from the membrane-distal extracellular domain (EC1) of boFcgamma2R corresponding to the homologous region of human FcalphaRI were synthesized. Binding of bovine IgG2 to the different peptides was tested by Dot-blot assay, and the peptide showing maximal binding was further modified by truncation and mutation. The minimum effective peptide 82FIGV85 located in the putative F-G loop of the EC1 domain was found to bind bovine IgG2 specifically and inhibit the binding of bovine IgG2 to the receptor. The Phe82, Ile83 and Val85 residues within the linear epitope were shown to be critical for IgG2-binding. Such functional epitope peptide should be very useful for understanding the IgG-Fcgamma interaction and development of FcR-targeting drugs.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zhang G,Guo J,Zhou J,Wang X,Li Q,Yang Y,Shen H,Zhao D,Zhang H,Xi J,Wang L,Qiao S,Jin Xdoi
10.1016/j.febslet.2006.01.060keywords:
subject
Has Abstractpub_date
2006-02-20 00:00:00pages
1383-90issue
5eissn
0014-5793issn
1873-3468pii
S0014-5793(06)00113-Xjournal_volume
580pub_type
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