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On-target IgG hexamerisation driven by a C-terminal IgM tail-piece fusion variant confers augmented complement activation

On-target IgG hexamerisation driven by a C-terminal IgM tail-piece fusion variant confers augmented complement activation
On-target IgG hexamerisation driven by a C-terminal IgM tail-piece fusion variant confers augmented complement activation

The majority of depleting monoclonal antibody (mAb) drugs elicit responses via Fc-FcγR and Fc-C1q interactions. Optimal C1q interaction is achieved through hexameric Fc:Fc interactions at the target cell surface. Herein is described an approach to exploit the tailpiece of the naturally multimeric IgM to augment hexamerisation of IgG. Fusion of the C-terminal tailpiece of IgM promoted spontaneous hIgG hexamer formation, resulting in enhanced C1q recruitment and complement-dependent cytotoxicity (CDC) but with off-target complement activation and reduced in-vivo efficacy. Mutation of the penultimate tailpiece cysteine to serine (C575S) ablated spontaneous hexamer formation, but facilitated reversible hexamer formation after concentration in solution. C575S mutant tailpiece antibodies displayed increased complement activity only after target binding, in-line with the concept of ‘on-target hexamerisation’, whilst retaining efficient in-vivo efficacy and augmented target cell killing in the lymph node. Hence, C575S-tailpiece technology represents an alternative format for promoting on-target hexamerisation and enhanced CDC.

2399-3642
Sopp, Joshua M.
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Peters, Shirley J.
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Rowley, Tania F.
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Oldham, Robert J.
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James, Sonya
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Mockridge, Ian
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French, Ruth R.
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Turner, Alison
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Beers, Stephen A.
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Humphreys, David P.
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Cragg, Mark S.
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Sopp, Joshua M.
d37f0a8c-ae5d-47cb-b7ce-bb7d58c9b88d
Peters, Shirley J.
9b1f5d1a-b4a0-44d1-9e03-319b97183398
Rowley, Tania F.
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Oldham, Robert J.
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James, Sonya
764c80e3-5bea-4b34-a871-b43f87ef97b0
Mockridge, Ian
327aef17-4837-4f2a-a93b-3d17cd1a7f9f
French, Ruth R.
a95ea7a1-7aeb-4c20-998e-fde663613fd1
Turner, Alison
de4cf092-66ae-40bc-89fd-2d8fb5214437
Beers, Stephen A.
a02548be-3ffd-41ab-9db8-d6e8c3b499a2
Humphreys, David P.
d65063fd-f745-4381-80b2-d2b5f673df04
Cragg, Mark S.
ec97f80e-f3c8-49b7-a960-20dff648b78c

Sopp, Joshua M., Peters, Shirley J., Rowley, Tania F., Oldham, Robert J., James, Sonya, Mockridge, Ian, French, Ruth R., Turner, Alison, Beers, Stephen A., Humphreys, David P. and Cragg, Mark S. (2021) On-target IgG hexamerisation driven by a C-terminal IgM tail-piece fusion variant confers augmented complement activation. Communications Biology, 4 (1), [1031]. (doi:10.1038/s42003-021-02513-3).

Record type: Article

Abstract

The majority of depleting monoclonal antibody (mAb) drugs elicit responses via Fc-FcγR and Fc-C1q interactions. Optimal C1q interaction is achieved through hexameric Fc:Fc interactions at the target cell surface. Herein is described an approach to exploit the tailpiece of the naturally multimeric IgM to augment hexamerisation of IgG. Fusion of the C-terminal tailpiece of IgM promoted spontaneous hIgG hexamer formation, resulting in enhanced C1q recruitment and complement-dependent cytotoxicity (CDC) but with off-target complement activation and reduced in-vivo efficacy. Mutation of the penultimate tailpiece cysteine to serine (C575S) ablated spontaneous hexamer formation, but facilitated reversible hexamer formation after concentration in solution. C575S mutant tailpiece antibodies displayed increased complement activity only after target binding, in-line with the concept of ‘on-target hexamerisation’, whilst retaining efficient in-vivo efficacy and augmented target cell killing in the lymph node. Hence, C575S-tailpiece technology represents an alternative format for promoting on-target hexamerisation and enhanced CDC.

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s42003-021-02513-3 - Version of Record
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Sopp et al. IgG On-Target IgG Hexamer Manuscript revised final acc
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More information

Accepted/In Press date: 2 August 2021
e-pub ahead of print date: 2 September 2021
Additional Information: Publisher Copyright: © 2021, The Author(s).

Identifiers

Local EPrints ID: 494118
URI: http://eprints.soton.ac.uk/id/eprint/494118
ISSN: 2399-3642
PURE UUID: 78bae6be-2b88-4cbb-aeb7-116c2dfcf671
ORCID for Robert J. Oldham: ORCID iD orcid.org/0000-0002-8007-1145
ORCID for Stephen A. Beers: ORCID iD orcid.org/0000-0002-3765-3342
ORCID for Mark S. Cragg: ORCID iD orcid.org/0000-0003-2077-089X

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Date deposited: 24 Sep 2024 16:42
Last modified: 03 Oct 2024 01:50

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Contributors

Author: Joshua M. Sopp
Author: Shirley J. Peters
Author: Tania F. Rowley
Author: Robert J. Oldham ORCID iD
Author: Sonya James
Author: Ian Mockridge
Author: Ruth R. French
Author: Alison Turner
Author: David P. Humphreys
Author: Mark S. Cragg ORCID iD

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