Evidence map›Paper›PMID 34698051›Full record

ArticleAntibodies (Basel, Switzerland)2021

Novel Selection Approaches to Identify Antibodies Targeting Neoepitopes on the C5b6 Intermediate Complex to Inhibit Membrane Attack Complex Formation.

Lasse Stach, Emily K H Dinley, Nadia Tournier, Ryan P Bingham, Darren A Gormley, Jo L Bramhall, Adam Taylor, Jane E Clarkson, Katherine A Welbeck, Claire L Harris and 6 more

Abstract read
In one paragraph

Article in Antibodies (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors.

Lasse StachBiopharm Discovery, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Emily K H DinleyBiopharm Discovery, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Nadia TournierBiopharm Discovery, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Ryan P BinghamScreening, Profiling and Mechanistic Biology, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Darren A GormleyImmunology Research Unit, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Jo L BramhallImmunology Research Unit, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Adam TaylorClinical Pharmacology & Experimental Medicine, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Jane E ClarksonBiopharm Discovery, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Katherine A WelbeckBiopharm Discovery, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Claire L HarrisImmunology Research Unit, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Maria FeeneyImmunology Research Unit, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.ORCID 0000-0001-6590-2927
Jane P HughesImmunology Research Unit, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Armin SeppSystems Modelling and Translational Biology, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Thil D BatuwangalaBiopharm Discovery, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Semra J KitchenImmunology Research Unit, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.
Eva-Maria NicholsImmunology Research Unit, GlaxoSmithKline, Gunnels Wood Road, Stevenage SG1 2NY, UK.ORCID 0000-0001-7636-6154

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The terminal pathway of complement is implicated in the pathology of multiple diseases and its inhibition is, therefore, an attractive therapeutic proposition. The practicalities of inhibiting this pathway, however, are challenging, as highlighted by the very few molecules in the clinic. The proteins are highly abundant, and assembly is mediated by high-affinity protein-protein interactions. One strategy is to target neoepitopes that are present transiently and only exist on active or intermediate complexes but not on the abundant native proteins. Here, we describe an antibody discovery campaign that generated neoepitope-specific mAbs against the C5b6 complex, a stable intermediate complex in terminal complement complex assembly. We used a highly diverse yeast-based antibody library of fully human IgGs to screen against soluble C5b6 antigen and successfully identified C5b6 neoepitope-specific antibodies. These antibodies were diverse, showed good binding to C5b6, and inhibited membrane attack complex (MAC) formation in a solution-based assay. However, when tested in a more physiologically relevant membrane-based assay these antibodies failed to inhibit MAC formation. Our data highlight the feasibility of identifying neoepitope binding mAbs, but also the technical challenges associated with the identification of functionally relevant, neoepitope-specific inhibitors of the terminal pathway.

Indexed as

antibody discoverycomplementneoepitopeterminal pathwaytherapeutic antibody

Identifiers

PMID34698051
PMCPMC8544208

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.