Evidence map›Paper›PMID 42294672›Full record

ArticlemBio2026

AlphaFold reveals how pathogenic

Abbie Hinds, Emily Johnson, Gareth Staton, Ferdinand N Njume, Hayley E Crosby-Durrani, Jarlath E Nally, Stuart Carter, Daniel J Rigden, Nicholas J Evans

Abstract read
In one paragraph

Article in mBio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

9 authors.

Abbie Hinds *Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Leahurst Campus, Chester, Neston, United Kingdom.ORCID 0000-0002-4108-7603
Emily Johnson *Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, United Kingdom.
Gareth StatonInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Leahurst Campus, Chester, Neston, United Kingdom.ORCID 0000-0003-4100-8597
Ferdinand N NjumeInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Leahurst Campus, Chester, Neston, United Kingdom.
Hayley E Crosby-DurraniInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Leahurst Campus, Chester, Neston, United Kingdom.
Jarlath E NallyInfectious Bacterial Disease Research Unit, National Animal Disease Centre, United States Department of Agriculture, Agricultural Research Service, Ames, Iowa, USA.ORCID 0000-0002-9478-1316
Stuart CarterInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Leahurst Campus, Chester, Neston, United Kingdom.
Daniel J Rigden *Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, United Kingdom.
Nicholas J Evans *Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Leahurst Campus, Chester, Neston, United Kingdom.ORCID 0000-0002-2950-1007

Funding

Biotechnology and Biological Sciences Research Council BB/W016133/1
6 · The paper itself

Abstract

Leptospirosis is a globally significant severe infectious disease that affects a range of mammals. To understand its complex aetiopathogenesis, IMPORTANCE: Leptospirosis is a globally important zoonotic disease of humans and animals, caused by the bacteria Leptospira. A central determinant of virulence is the ability for these bacteria to evade complement, a host defense system that assembles the membrane attack complex to eliminate pathogens. Here, we elucidate a novel immune evasion mechanism in which the leptospiral surface protein LIC13259 forms a disulfide bond with complement component C8γ, preventing binding of C8α. This interaction disrupts the membrane attack complex assembly and promotes bacterial survival. To our knowledge, this represents the first example of a cross-kingdom disulfide bond mediating bacterial pathogenesis. These findings provide novel insights into leptospiral immune modulation and demonstrate the power of AlphaFold-based structural predictions to reveal unique host-pathogen interactions.

Indexed as

Complement C8Complement Membrane Attack ComplexDisulfidesImmune EvasionLeptospiraSulfhydryl CompoundsAnimalsBacterial AdhesionHumansLeptospirosisLipoproteinsModels, MolecularProtein BindingComplement C8Complement Membrane Attack ComplexDisulfidesLipoproteinsSulfhydryl CompoundsAlphaFold2complement evasioncross-kingdomhost-pathogen interactionsLeptospiramembrane attack complex (MAC)thiol-disulfide exchange

Identifiers

PMID42294672
PMCPMC13344006

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.