Evidence map›Paper›PMID 42500807›Full record

ArticleRSC chemical biology2026

Ant abaecin-2 is a context-dependent copper-binding effector that can be either inhibitory or protective.

Caroline M Donaghy, Helena V Heyer-Gray, Charlotte O'Hern, Michael Ibrahim, Bryant Perez-Torres, Nichali Bogues, Andrei T Alexandrescu, Karrera Y Djoko, Jonathan L Klassen, Alfredo M Angeles-Boza

Abstract read
In one paragraph

Article in RSC chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Caroline M DonaghyDepartment of Chemistry, University of Connecticut Storrs Connecticut USA alfredo.angeles-boza@uconn.edu.ORCID https://orcid.org/0000-0002-9746-9440
Helena V Heyer-GrayDepartment of Molecular and Cell Biology, University of Connecticut Storrs Connecticut USA jonathan.klassen@uconn.edu.ORCID https://orcid.org/0000-0003-1119-0893
Charlotte O'HernDepartment of Biosciences Durham University, Durham UK karrera.djoko@durham.ac.uk.
Michael IbrahimDepartment of Chemistry, University of Connecticut Storrs Connecticut USA alfredo.angeles-boza@uconn.edu.
Bryant Perez-TorresDepartment of Chemistry, University of Connecticut Storrs Connecticut USA alfredo.angeles-boza@uconn.edu.
Nichali BoguesDepartment of Chemistry, University of Connecticut Storrs Connecticut USA alfredo.angeles-boza@uconn.edu.
Andrei T AlexandrescuDepartment of Molecular and Cell Biology, University of Connecticut Storrs Connecticut USA jonathan.klassen@uconn.edu.
Karrera Y DjokoDepartment of Biosciences Durham University, Durham UK karrera.djoko@durham.ac.uk.ORCID https://orcid.org/0000-0001-9814-6515
Jonathan L KlassenDepartment of Molecular and Cell Biology, University of Connecticut Storrs Connecticut USA jonathan.klassen@uconn.edu.ORCID https://orcid.org/0000-0003-1745-8838
Alfredo M Angeles-BozaDepartment of Chemistry, University of Connecticut Storrs Connecticut USA alfredo.angeles-boza@uconn.edu.ORCID https://orcid.org/0000-0002-5560-4405

Funding

An Open-access 800 MHz NMR Spectrometer for Central New EnglandS10RR023041 · NCRR · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI HOCH, JEFFREY C · 2007 to 2007
$2.0M
An Open-access 700 MHz NMR Spectrometer for Central New EnglandS10OD034297 · OD · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI HOCH, JEFFREY C · 2023 to 2023
$2.0M
NCRR NIH HHS S10 RR023041NIH HHS S10 OD034297
6 · The paper itself

Abstract

Host defense peptides (HDPs) are important components of the innate immune system that are used to combat pathogens and often rely on binding trace nutrient metals for their function. However, controlling nutrient metals may have other roles in host-symbiont interactions beyond poisoning harmful pathogens. This study characterizes the evolution, structural properties, and biochemical activity of the novel hymenopteran HDP abaecin-2. In myrmicine ants such as the fungus-growing tribe Attini, abaecin-2 has evolved to include an Amino-Terminal Cu(ii) and Ni(ii)-binding (ATCUN) motif, which we hypothesize binds copper, a trace nutrient that is enriched in attine ant colonies. Combined results from mass spectrometry, competitive binding assays, circular dichroism, and NMR indicate that the abaecin-2 peptide lacks a defined secondary structure and can associate with up to 2 Cu(ii) ions, one strongly bound at the ATCUN motif and another weakly bound, likely at a conserved histidine residue. Despite its copper-binding activity, abaecin-2 alone does not exhibit antibacterial activity against

Identifiers

PMID42500807
PMCPMC13398410

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LicenceCC BY
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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.