Glycan-independent binding and internalization of human IgG to FCMR, its cognate cellular receptory

Lloyd, Katy, Wang, Jiabin, Urban, Britta ORCID: https://orcid.org/0000-0002-4197-8393, Czajkowsky, Daniel and Pleass, Richard ORCID: https://orcid.org/0000-0001-7438-8296 (2017) 'Glycan-independent binding and internalization of human IgG to FCMR, its cognate cellular receptory'. Scientific Reports, Vol 7, e42989.

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Abstract

IgM is the first antibody to be produced in immune responses and plays an important role in the neutralization of bacteria and viruses. Human IgM is heavily glycosylated, featuring five N-linked glycan sites on the μ chain and one on the J-chain. Glycosylation of IgG is known to modulate the effector functions of Fcγ receptors. In contrast, little is known about the effect of glycosylation on IgM binding to the human Fcμ receptor (hFCMR). In this study, we identify the Cμ, omain of IgM as the target of hFCMR, and show that binding and internalization of IgM by hFCMR is glycan-independent. We generated a homology-based structure for hFCMR and used molecular dynamic simulations to show how this interaction with IgM may occur. Finally, we reveal an inhibitory function for IgM in the proliferation of T cells.

Item Type:	Article
Subjects:	QW Microbiology and Immunology > Reference Works. General Immunology > QW 520 Research (General) QW Microbiology and Immunology > Antigens and Antibodies. Toxins and Antitoxins > QW 575 Antibodies QW Microbiology and Immunology > Immune Responses > QW 700 Infection. Mechanisms of infection and resistance.
Faculty: Department:	Biological Sciences > Department of Tropical Disease Biology
Digital Object Identifer (DOI):	https://doi.org/10.1038/srep42989
Depositing User:	Mary Creegan
Date Deposited:	08 Mar 2017 15:22
Last Modified:	06 Feb 2018 13:14
URI:	https://archive.lstmed.ac.uk/id/eprint/6821

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