The University of Southampton
University of Southampton Institutional Repository

Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions

Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions
Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions

Antibodies contain a conserved glycosylation site that has emerged as a target for the modulation of antibody effector functions. The crystal structure of a biosynthetic intermediate of human IgG1, bearing immature oligomannose-type glycans and reported to display increased antibody-dependent cellular cytotoxicity, demonstrates that glycan engineering can bias the Fc to an open conformation primed for receptor binding.

antibody, antibody engineering, glycosylation, kifunensine, oligomannose
0022-2836
1061-1066
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Bowden, Thomas A.
4b17a588-ac01-4112-807a-8b99a6c20d0f
Coles, Charlotte H.
8c3ba446-999e-431a-8a4c-aab4ccd3b2dc
Harlos, Karl
b5f7d1ec-d765-4d39-b8f2-65c6917f1d21
Aricescu, A. Radu
8ee3d2bd-7ef7-4e85-862a-e13f48ae0fa6
Harvey, David J.
8bb24417-3852-4b1f-827b-0d5d2c176744
Stuart, David I.
2751c230-9d4c-4981-aeb7-cafb51ed749d
Jones, E. Yvonne
6b9004c9-137b-4f43-8a14-c7c83bcaa4be
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Bowden, Thomas A.
4b17a588-ac01-4112-807a-8b99a6c20d0f
Coles, Charlotte H.
8c3ba446-999e-431a-8a4c-aab4ccd3b2dc
Harlos, Karl
b5f7d1ec-d765-4d39-b8f2-65c6917f1d21
Aricescu, A. Radu
8ee3d2bd-7ef7-4e85-862a-e13f48ae0fa6
Harvey, David J.
8bb24417-3852-4b1f-827b-0d5d2c176744
Stuart, David I.
2751c230-9d4c-4981-aeb7-cafb51ed749d
Jones, E. Yvonne
6b9004c9-137b-4f43-8a14-c7c83bcaa4be

Crispin, Max, Bowden, Thomas A., Coles, Charlotte H., Harlos, Karl, Aricescu, A. Radu, Harvey, David J., Stuart, David I. and Jones, E. Yvonne (2009) Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions. Journal of Molecular Biology, 387 (5), 1061-1066. (doi:10.1016/j.jmb.2009.02.033).

Record type: Article

Abstract

Antibodies contain a conserved glycosylation site that has emerged as a target for the modulation of antibody effector functions. The crystal structure of a biosynthetic intermediate of human IgG1, bearing immature oligomannose-type glycans and reported to display increased antibody-dependent cellular cytotoxicity, demonstrates that glycan engineering can bias the Fc to an open conformation primed for receptor binding.

This record has no associated files available for download.

More information

Published date: 17 April 2009
Keywords: antibody, antibody engineering, glycosylation, kifunensine, oligomannose

Identifiers

Local EPrints ID: 414586
URI: http://eprints.soton.ac.uk/id/eprint/414586
ISSN: 0022-2836
PURE UUID: 36463085-f997-45e0-8159-985cf2a14b04
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 04 Oct 2017 16:30
Last modified: 16 Mar 2024 04:30

Export record

Altmetrics

Contributors

Author: Max Crispin ORCID iD
Author: Thomas A. Bowden
Author: Charlotte H. Coles
Author: Karl Harlos
Author: A. Radu Aricescu
Author: David J. Harvey
Author: David I. Stuart
Author: E. Yvonne Jones

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×