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Default NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein.

NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein.

Related Articles NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein.

Biomol NMR Assign. 2021 Jan 10;:

Authors: Yanaka S, Yamaguchi Y, Takizawa T, Miyanoiri Y, Yogo R, Shimada I, Kato K

Abstract
The Fc portion of immunoglobulin G (IgG) promotes defensive effector functions in the immune system by interacting with Fc? receptors and complement component C1q. These interactions critically depend on N-glycosylation at Asn297 of each CH2 domain, where biantennary complex-type oligosaccharides contain microheterogeneities resulting primarily from the presence or absence of non-reducing terminal galactose residues. Crystal structures of Fc have shown that a pair of N-glycans is located between the two CH2 domains. Here we applied our metabolic isotope labeling technique using mammalian cells for in-solution structural characterization of mouse IgG2b-Fc glycoforms with a molecular mass of 54*kDa. Based on spectral assignments of the N-glycans as well as polypeptide backbones of Fc, we probed conformational perturbations of Fc induced by N-glycan trimming, especially enzymatic degalactosylation. The results indicated that degalactosylation structurally perturbed the Fc region through rearrangement of glycan-protein interactions. The spectral assignments of IgG2b-Fc glycoprotein will provide the basis for NMR investigation of its dynamic conformations and interactions with effector molecules in solution.


PMID: 33423189 [PubMed - as supplied by publisher]



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