Identification of the Linear Fc-Binding Site on the Bovine IgG1 Fc Receptor (boFcγRIII) Using Synthetic Peptides
文献类型: 外文期刊
第一作者: Wang, Ruining
作者: Wang, Ruining;Guo, Junqing;Yang, Jifei;Li, Qingmei;Zhang, Gaiping;Wang, Ruining;Li, Ge;Wang, Xun;Zhang, Gaiping;Zhang, Gaiping
作者机构:
关键词: BoFc gamma RIII; Fc-binding site; bovine IgG1; synthetic peptides
期刊名称:VETERINARY SCIENCES ( 影响因子:2.4; )
ISSN:
年卷期: 2024 年 11 卷 1 期
页码:
收录情况: SCI
摘要: The bovine IgG1 Fc receptor (boFc gamma RIII) is a homologue to human Fc gamma RIII (CD16) that binds bovine IgGI with medium-low affinity. In order to identify the Fc-binding site on the bovine IgG1 Fc receptor (boFc gamma RIII), peptides derived from the second extracellular domain (EC2) of boFc gamma RIII were synthesized and conjugated with the carrier protein. With a Dot-blot assay, the ability of the peptides to bind bovine IgG1 was determined, and the IgG1-binding peptide was also identified via truncation and mutation. The minimal peptide AQRVVN corresponding to the sequence 98-103 of boFc gamma RIII bound bovine IgG1 in Dot-blot, suggesting that it represents a linear ligand-binding site located in the putative A-B loop of the boFc gamma RIII EC2 domain. Mutation analysis of the peptide showed that the residues of Ala(98), Gln(99), Val(101), Val(102) and Asn(103) within the Fc-binding site are critical for IgG1 binding on boFc gamma RIII. The functional peptide identified in this paper is of great value to the IgG-Fc interaction study and FcR-targeting drug development.
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