Journal: MAbs / Year: 2019 Title: C2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering. Authors: Seiki Yageta / Hiroshi Imamura / Risa Shibuya / Shinya Honda / Abstract: The N-linked glycan in immunoglobulin G is critical for the stability and function of the crystallizable fragment (Fc) region. Alteration of these protein properties upon the removal of the N-linked ...The N-linked glycan in immunoglobulin G is critical for the stability and function of the crystallizable fragment (Fc) region. Alteration of these protein properties upon the removal of the N-linked glycan has often been explained by the alteration of the C2 domain orientation in the Fc region. To confirm this hypothesis, we examined the small-angle X-ray scattering (SAXS) profile of the glycosylated Fc region (gFc) and aglycosylated Fc region (aFc) in solution. Conformational characteristics of the C2 domain orientation were validated by comparison with SAXS profiles theoretically calculated from multiple crystal structures of the Fc region with different C2 domain orientations. The reduced chi-square values from the fitting analyses of gFc and aFc associated with the degree of openness or closure of each crystal structure, as determined from the first principal component that partially governed the variation of the C2 domain orientation extracted by a singular value decomposition analysis. For both gFc and aFc, the best-fitted SAXS profiles corresponded to ones calculated based on the crystal structure of gFc that formed a "semi-closed" C2 domain orientation. Collectively, the data indicated that the removal of the N-linked glycan only negligibly affected the C2 domain orientation in solution. These findings will guide the development of methodology for the production of highly refined functional Fc variants.
Contact author
Seiki Yageta (AIST, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan)
Instrument name: Photon Factory (PF), High Energy Accelerator Research Organization (KEK) BL-10C City: Tsukuba / 国: Japan / Type of source: X-ray synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 2 mm
Detector
Name: Pilatus3 2M / Pixsize x: 0.172 mm
Scan
Title: Glycosylated Human Immunoglobulin G Fc Region / Measurement date: Mar 5, 2017 / Cell temperature: 25 °C / Exposure time: 2 sec. / Number of frames: 15 / Unit: 1/A /
Min
Max
Q
0.0101
0.3497
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 331 /
Min
Max
Q
0.019196
0.296245
P(R) point
1
331
R
0
102.1
Result
Type of curve: single_conc /
Experimental
Standard
Porod
MW
53.7 kDa
53.7 kDa
-
Volume
-
-
66 nm3
P(R)
Guinier
Guinier error
Forward scattering, I0
2052
0.039
-
Radius of gyration, Rg
2.79 nm
2.744 nm
0.15
Min
Max
D
-
10.21
Guinier point
43
187
+
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