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Molecular cloning and identification of full-length cDNA encoding high affinity Fc receptor for bovine IgG (Fc gamma RI).

作者信息

Yan Y, Li X, Wang A, Zhang G

机构信息

Institute of Animal and Veterinary Sciences, Henan Academy of Agricultural Sciences, 450002, Zhengzhou, China.

出版信息

Vet Immunol Immunopathol. 2000 Jun 30;75(1-2):151-9. doi: 10.1016/s0165-2427(00)00197-5.

DOI:10.1016/s0165-2427(00)00197-5
PMID:10889306
Abstract

The receptor I for the Fc region of immunoglobulin G (Fc gamma RI) is a member of the Ig superfamily with a high affinity, and it mediates antibody-dependent cellular cytotoxicity and immune complex clearance. In this study, a cDNA encoding the bovine Fc gamma RI was cloned. The full-length cDNA sequence is 1050 bp long with a short 5'- and long 3'-untranslated end regions, which codes for 349 amino acids and contains a signal peptide, an extracellular region with three Ig-like domains, and transmembrane and intracytoplasmic domains. Five potential N-linked glycosylation sites are recognized in this sequence. Compared with the sequences of human and mouse Fc gamma RI, the homologies of nucleotide sequences are 80 and 69% and homologies of deduced amino acid sequences are 66 and 55%, respectively. It is shown that the sequences of the monomeric IgG binding domain in these three species of Fc gamma RI are highly conserved.

摘要

相似文献

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