Correlation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition

Aim: Fragment crystallizable (Fc) glycans modulate Fc conformations and functions, and glycan may also regulate antigen recognition. In the antibody drug development, glycosylation patterns affect antibody drug characteristics and quality control. In order to provide a global feature of N-glycan int...

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Autor principal:	Buyong Ma
Formato:	article
Lenguaje:	EN
Publicado:	Open Exploration Publishing Inc. 2021
Materias:	antigen recognition molecular dynamics simulations allosteric glycan fc receptor binding antibody drug Immunologic diseases. Allergy RC581-607
Acceso en línea:	https://doaj.org/article/2648c22de1f94d2b8358476e0101f6aa
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spelling	oai:doaj.org-article:2648c22de1f94d2b8358476e0101f6aa2021-11-24T01:40:52ZCorrelation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition10.37349/ei.2021.000042768-6655https://doaj.org/article/2648c22de1f94d2b8358476e0101f6aa2021-04-01T00:00:00Zhttps://www.explorationpub.com/Journals/ei/Article/10034https://doaj.org/toc/2768-6655Aim: Fragment crystallizable (Fc) glycans modulate Fc conformations and functions, and glycan may also regulate antigen recognition. In the antibody drug development, glycosylation patterns affect antibody drug characteristics and quality control. In order to provide a global feature of N-glycan interactions in response to antigen and Fc receptor bindings, the interactions among Fc N-glycans and N-glycans’ interaction with Fc CH2 and CH3 domains have been studied. Methods: Molecular dynamics simulations were used to generate conformation ensembles of free antibody, antibody-antigen complex, antibody-human Fc-gamma-receptor-I (hFcγRI) and antibody-antigen-hFcγRI, the hydrogen bonds and radial distance distribution involving N-glycans carbohydrate chains have been analyzed. Results: Two important interaction patterns have been observed. The first is the strong but non-specific interactions between two carbohydrate chains in free antibody. Secondly, it has been found that N-glycans carbohydrate chains can directly interact with CH3 domain in free antibody, and that the distance distribution between carbohydrate chains and CH3 domain clearly differentiate the free antibody, antibody-antigen complex, antibody-hFcγRI complex, and final antibody-antigen-hFcγRI complex. Conclusions: N-glycans partially acts as allosteric sensor and respond to antigen and hFcγRI binding.Buyong MaOpen Exploration Publishing Inc.articleantigen recognitionmolecular dynamics simulationsallostericglycanfc receptor bindingantibody drugImmunologic diseases. AllergyRC581-607ENExploration of Immunology, Vol 1, Iss 1, Pp 27-36 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	antigen recognition molecular dynamics simulations allosteric glycan fc receptor binding antibody drug Immunologic diseases. Allergy RC581-607
spellingShingle	antigen recognition molecular dynamics simulations allosteric glycan fc receptor binding antibody drug Immunologic diseases. Allergy RC581-607 Buyong Ma Correlation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition
description	Aim: Fragment crystallizable (Fc) glycans modulate Fc conformations and functions, and glycan may also regulate antigen recognition. In the antibody drug development, glycosylation patterns affect antibody drug characteristics and quality control. In order to provide a global feature of N-glycan interactions in response to antigen and Fc receptor bindings, the interactions among Fc N-glycans and N-glycans’ interaction with Fc CH2 and CH3 domains have been studied. Methods: Molecular dynamics simulations were used to generate conformation ensembles of free antibody, antibody-antigen complex, antibody-human Fc-gamma-receptor-I (hFcγRI) and antibody-antigen-hFcγRI, the hydrogen bonds and radial distance distribution involving N-glycans carbohydrate chains have been analyzed. Results: Two important interaction patterns have been observed. The first is the strong but non-specific interactions between two carbohydrate chains in free antibody. Secondly, it has been found that N-glycans carbohydrate chains can directly interact with CH3 domain in free antibody, and that the distance distribution between carbohydrate chains and CH3 domain clearly differentiate the free antibody, antibody-antigen complex, antibody-hFcγRI complex, and final antibody-antigen-hFcγRI complex. Conclusions: N-glycans partially acts as allosteric sensor and respond to antigen and hFcγRI binding.
format	article
author	Buyong Ma
author_facet	Buyong Ma
author_sort	Buyong Ma
title	Correlation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition
title_short	Correlation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition
title_full	Correlation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition
title_fullStr	Correlation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition
title_full_unstemmed	Correlation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition
title_sort	correlation of n-glycan dynamics and interaction network with allosteric antigen binding and fc receptor recognition
publisher	Open Exploration Publishing Inc.
publishDate	2021
url	https://doaj.org/article/2648c22de1f94d2b8358476e0101f6aa
work_keys_str_mv	AT buyongma correlationofnglycandynamicsandinteractionnetworkwithallostericantigenbindingandfcreceptorrecognition
_version_	1718416023441375232

Correlation of N-glycan dynamics and interaction network with allosteric antigen binding and Fc receptor recognition

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