Evidence map›Paper›PMID 36513069›Full record

ArticleStructure (London, England : 1993)2023

Structures of drug-specific monoclonal antibodies bound to opioids and nicotine reveal a common mode of binding.

Justas V Rodarte, Carly Baehr, Dustin Hicks, Tyler L Liban, Connor Weidle, Peter B Rupert, Rajwana Jahan, Abigail Wall, Andrew T McGuire, Roland K Strong and 3 more

Open access · greenAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. PMA exerts anti-leukemia effect in PhCancer cell international · 2025
    Article
  3. Review
  4. Article
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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

13 authors at 5 institutions in 1 country.

Justas V RodarteVaccine and Infectious Disease Division, Fred Hutchinson Cancer Center, Seattle, WA, USA.
Carly BaehrDepartment of Pharmacology, University of Minnesota Medical School, Minneapolis, MN, USA.
Dustin HicksDepartment of Pharmacology, University of Minnesota Medical School, Minneapolis, MN, USA.
Tyler L LibanVaccine and Infectious Disease Division, Fred Hutchinson Cancer Center, Seattle, WA, USA.
Connor WeidleVaccine and Infectious Disease Division, Fred Hutchinson Cancer Center, Seattle, WA, USA.
Peter B RupertBasic Science Division, Fred Hutchinson Cancer Center, Seattle, WA, USA.
Rajwana JahanResearch Triangle Institute International, Research Triangle Park, Durham, NC, USA.
Abigail WallVaccine and Infectious Disease Division, Fred Hutchinson Cancer Center, Seattle, WA, USA.
Andrew T McGuireVaccine and Infectious Disease Division, Fred Hutchinson Cancer Center, Seattle, WA, USA; Department of Global Health, University of Washington, Seattle, WA, USA; Department of Laboratory Medicine and Pathology, University of Washington, Seattle, WA, USA.
Roland K StrongBasic Science Division, Fred Hutchinson Cancer Center, Seattle, WA, USA.
Scott RunyonResearch Triangle Institute International, Research Triangle Park, Durham, NC, USA.
Marco PravetoniDepartment of Pharmacology, University of Minnesota Medical School, Minneapolis, MN, USA; Department of Psychiatry and Behavioral Sciences, Department of Pharmacology, School of Medicine, University of Washington, Seattle, WA, USA; Center for Medication Development for Substance Use Disorders and Overdose, University of Washington, Seattle, WA, USA. Electronic address: mprave@uw.edu.
Marie PanceraVaccine and Infectious Disease Division, Fred Hutchinson Cancer Center, Seattle, WA, USA. Electronic address: mpancera@fredhutch.org.
Fred Hutch Cancer Center · USRTI International · USUniversity of Minnesota Medical Center · USInfectious Disease Research Institute · USUniversity of Washington · US

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Gregory L Hura · 2017 to 2026
$28.6M
Phase 1a/1b Clinical Trials of Multivalent Opioid Vaccine ComponentsUG3DA047711 · NIDA · NEW YORK STATE PSYCHIATRIC INSTITUTE DBA RESEARCH FOUNDATION FOR MENTAL HYGIENE, INC · PI COMER, SANDRA D, PRAVETONI, MARCO · 2018 to 2019
$9.4M
Development of a monoclonal antibody to reverse overdose from fentanyl and its analogs: from manufacturing to clinical trialsUG3DA057850 · NIDA · UNIVERSITY OF WASHINGTON · PI COMER, SANDRA D, PRAVETONI, MARCO · 2022 to 2022
$8.3M
Phase 1a/1b Clinical Trials of Multivalent Opioid Vaccine ComponentsUH3DA047711 · NIDA · NEW YORK STATE PSYCHIATRIC INSTITUTE DBA RESEARCH FOUNDATION FOR MENTAL HYGIENE, INC · PI SANDRA D. COMER, Marco Pravetoni · 2023 to 2026
$7.3M
ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
Antibody-based countermeasures against fentanyl and its analoguesU01DA051658 · NIDA · UNIVERSITY OF WASHINGTON · PI PRAVETONI, MARCO · 2020 to 2022
$2.4M
Pilatus 6mS10OD021832 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI ADAMS, PAUL DAVID · 2016 to 2016
$980k
Howard Hughes Medical InstituteNIDA NIH HHS U01 DA051658NIDA NIH HHS UG3 DA047711NIDA NIH HHS UG3 DA057850NIDA NIH HHS UH3 DA047711NIGMS NIH HHS P30 GM124169NIGMS NIH HHS R01 GM129325NIH HHS S10 OD021832
6 · The paper itself

Abstract

Opioid-related fatal overdoses have reached epidemic proportions. Because existing treatments for opioid use disorders offer limited long-term protection, accelerating the development of newer approaches is critical. Monoclonal antibodies (mAbs) are an emerging treatment strategy that targets and sequesters selected opioids in the bloodstream, reducing drug distribution across the blood-brain barrier, thus preventing or reversing opioid toxicity. We previously identified a series of murine mAbs with high affinity and selectivity for oxycodone, morphine, fentanyl, and nicotine. To determine their binding mechanism, we used X-ray crystallography to solve the structures of mAbs bound to their respective targets, to 2.2 Å resolution or higher. Structural analysis showed a critical convergent hydrogen bonding mode that is dependent on a glutamic acid residue in the mAbs' heavy chain and a tertiary amine of the ligand. Characterizing drug-mAb complexes represents a significant step toward rational antibody engineering and future manufacturing activities to support clinical evaluation.

Indexed as

Analgesics, OpioidNicotineAnimalsAntibodies, MonoclonalMiceMorphineOxycodoneAnalgesics, OpioidAntibodies, MonoclonalMorphineNicotineOxycodonecrystal structurefentanylligandsmAbsmorphinenicotineopioid use disorderoxycodonevaccine

Identifiers

PMID36513069
PMCPMC12039075
OpenAlexW4311227720

What OpenQuestion holds

Textmetadata
LicenceTDM
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.