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Journal article

Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis

Abstract:

Human IgG Fc glycosylation modulates immunological effector functions such as antibody-dependent cellular cytotoxicity and phagocytosis. Engineering of Fc glycans therefore enables fine-tuning of the therapeutic properties of monoclonal antibodies. The N-linked glycans of Fc are typically complex-type, forming a network of noncovalent interactions along the protein surface of the Cγ2 domain. Here, we manipulate the mammalian glycan-processing pathway to trap IgG1 Fc at sequential stages of ma...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/ja306068g

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Funding agency for:
Bowden, T
Grant:
089026/Z/09/Z
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Funding agency for:
Aricescu, A
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Funding agency for:
Jones, E
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Publisher:
American Chemical Society Publisher's website
Journal:
Journal of the American Chemical Society Journal website
Volume:
134
Issue:
42
Pages:
17554-17563
Publication date:
2012-10-01
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
Source identifiers:
353920
Language:
English
Keywords:
Pubs id:
pubs:353920
UUID:
uuid:4f06077c-53dd-4e36-b0bf-9be13bba144c
Local pid:
pubs:353920
Deposit date:
2013-11-16

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