The effect of sugar removal on the structure of the Fc region of an IgG antibody as observed with single molecule Forster Resonance Energy Transfer

被引：7

作者：

Kelliher, Michael T. ^{[1
]}

Jacks, Ramiah D. ^{[1
]}

Piraino, Mark S. ^{[1
]}

Southern, Cathrine A. ^{[1
]}

机构：

[1] Depaul Univ, Dept Chem, Chicago, IL 60614 USA

来源：

MOLECULAR IMMUNOLOGY | 2014年 / 60卷 / 02期

关键词：

Forster Resonance Energy Transfer; Single molecule; Fc degylcosylation; IgG structure; ENDOGLYCOSIDASE ENDOS; SPECTROSCOPIC RULER; GAMMA-RI; GLYCOSYLATION; PROTEIN; FRET; CARBOHYDRATE; INFLAMMATION; GLYCOFORMS; RECEPTORS;

D O I：

10.1016/j.molimm.2014.04.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The deglycosylation of immunoglobulin G (IgG) antibodies leads to a diminished immune response. This reduction in immune response is thought to arise from weakened binding of IgG antibodies to effector molecules as a result of a conformational change in the antibody. The nature of this structural alteration is uncertain due to the conflicting results obtained from different experimental methods. We have examined the impact of deglycosylation by the endoglycosidase PNGase Fan the structure of the Fc region of a human IgG antibody using single molecule Forster Resonance Energy Transfer (FRET). The FRET efficiency histograms obtained indicate that the structure of the Fc region becomes more flexible upon deglycosylation. This is demonstrated by a change in the width of the energy transfer efficiency peak, which increases from 0.19 +/- 0.02 to 0.6 +/- 0.1 upon deglycosylation. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：103 / 108

页数：6

共 36 条

[21] The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms [J].