Evidence map›Paper›PMID 36797260›Full record

ArticleNature communications2023

Structural basis for membrane attack complex inhibition by CD59.

Emma C Couves, Scott Gardner, Tomas B Voisin, Jasmine K Bickel, Phillip J Stansfeld, Edward W Tate, Doryen Bubeck

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
10.8field-weighted citation impact, top 1% of its field
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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.

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  18. Molecular characterization ofOpen veterinary journal · 2026
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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

7 authors at 2 institutions in 1 country.

Emma C CouvesDepartment of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, United Kingdom.
Scott GardnerDepartment of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, United Kingdom.
Tomas B VoisinDepartment of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, United Kingdom.
Jasmine K BickelDepartment of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, United Kingdom.
Phillip J StansfeldSchool of Life Sciences and Department of Chemistry, Gibbet Hill Campus, The University of Warwick, Coventry, CV4 7AL, United Kingdom.ORCID 0000-0001-8800-7669
Edward W TateDepartment of Chemistry, Molecular Sciences Research Hub, Imperial College London, London, W12 0BZ, United Kingdom.ORCID 0000-0003-2213-5814
Doryen BubeckDepartment of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, United Kingdom. d.bubeck@imperial.ac.uk.ORCID 0000-0001-8241-9697
Imperial College London · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MR/S009213/1Wellcome Trust
6 · The paper itself

Abstract

CD59 is an abundant immuno-regulatory receptor that protects human cells from damage during complement activation. Here we show how the receptor binds complement proteins C8 and C9 at the membrane to prevent insertion and polymerization of membrane attack complex (MAC) pores. We present cryo-electron microscopy structures of two inhibited MAC precursors known as C5b8 and C5b9. We discover that in both complexes, CD59 binds the pore-forming β-hairpins of C8 to form an intermolecular β-sheet that prevents membrane perforation. While bound to C8, CD59 deflects the cascading C9 β-hairpins, rerouting their trajectory into the membrane. Preventing insertion of C9 restricts structural transitions of subsequent monomers and indirectly halts MAC polymerization. We combine our structural data with cellular assays and molecular dynamics simulations to explain how the membrane environment impacts the dual roles of CD59 in controlling pore formation of MAC, and as a target of bacterial virulence factors which hijack CD59 to lyse human cells.

Indexed as

Complement C9Complement Membrane Attack ComplexCD59 AntigensComplement ActivationComplement C8Cryoelectron MicroscopyHumansCD59 AntigensCD59 protein, humanComplement C8Complement C9Complement Membrane Attack Complex

Identifiers

PMID36797260
PMCPMC9935631
OpenAlexW4321078922

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.