TAILIEUCHUNG - Báo cáo khoa học: Ligand binding and antigenic properties of a human neonatal Fc receptor with mutation of two unpaired cysteine residues

The neonatal Fc receptor (FcRn) is a major histocompatibility complex class I-related molecule that regulates the half-life of IgG and albumin. In addition, FcRn directs the transport of IgG across both mucosal epithe-lium and placenta and also enhances phagocytosis in neutrophils. This new knowledge gives incentives for the design of IgG and albumin-based diag-nostics and therapeutics. | ỊFEBS Journal Ligand binding and antigenic properties of a human neonatal Fc receptor with mutation of two unpaired cysteine residues Jan T. Andersen1 Sune Justesen2 Burkhard Fleckenstein3 Terje E. Michaelsen4 5 G0ril Berntzen1 Vania E. Kenanova6 Muluneh B. Daba1 Vigdis Lauvrak1 S0ren Buus2 and Inger Sandlie1 1 Department of Molecular Biosciences and Centre for Immune Regulation University of Oslo Norway 2 Institute of MedicalMicrobiology and Immunology University of Copenhagen Denmark 3 Institute of Immunology and Centre for Immune Regulation University of Oslo Rikshospitalet University Hospital Norway 4 Norwegian Institute of Public Health Oslo Norway 5 Institute of Pharmacy University of Oslo Norway 6 Crump Institute for Molecular Imaging Department of Molecular and MedicalPharmacology David Geffen Schoolof Medicine at University of California Los Angeles USA Keywords antigenic properties bacterialexpression MALDI-TOF peptide mapping soluble human neonatalFc receptor shFcRn unpaired cysteines Correspondence J. T. Andersen Department of Molecular Biosciences University of Oslo PO Box 1041 0316 Oslo Norway Fax 47 22 85 40 61 Tel 47 22 85 47 93 E-mail janta@ Present address Norwegian Knowledge Centre for the Health Services Oslo Norway Received 11 April2008 revised 6 June 2008 accepted 13 June 2008 doi The neonatal Fc receptor FcRn is a major histocompatibility complex class I-related molecule that regulates the half-life of IgG and albumin. In addition FcRn directs the transport of IgG across both mucosal epithelium and placenta and also enhances phagocytosis in neutrophils. This new knowledge gives incentives for the design of IgG and albumin-based diagnostics and therapeutics. To study FcRn in vitro and to select and characterize FcRn binders large quantities of soluble human FcRn are needed. In this report we explored the impact of two free cysteine residues C48 and C251 of the FcRn heavy .

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