Evidence map›Paper›PMID 40632652›Full record

ArticleCell reports2025

In situ insights into antibody-mediated neutralization of a pre-fusion Junin virus glycoprotein complex.

Lily J Taylor, Michael R Sawaya, Jonna B Westover, Chenyi Wang, Frederick Jimenez, Aldo J Muñoz, Julian Whitelegge, Brian B Gowen, Gustavo F Helguera, Roger Castells-Graells and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

11 authors.

Lily J TaylorDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, California, Los Angeles (UCLA), Los Angeles, CA 90095, USA. Electronic address: lilyjanetaylor@g.ucla.edu.
Michael R SawayaDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Jonna B WestoverDepartment of Animal, Dairy and Veterinary Sciences, Utah State University, Logan, UT 84322, USA.
Chenyi WangThe Pasarow Mass Spectrometry Laboratory, The Jane and Terry Semel Institute for Neuroscience and Human Behavior, David Geffen School of Medicine, University of California, California (UCLA), Los Angeles, CA, USA.
Frederick JimenezDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Aldo J MuñozDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Julian WhiteleggeThe Pasarow Mass Spectrometry Laboratory, The Jane and Terry Semel Institute for Neuroscience and Human Behavior, David Geffen School of Medicine, University of California, California (UCLA), Los Angeles, CA, USA.
Brian B GowenDepartment of Animal, Dairy and Veterinary Sciences, Utah State University, Logan, UT 84322, USA. Electronic address: brian.gowen@usu.edu.
Gustavo F HelgueraLaboratory of Pharmaceutical Biotechnology, Instituto de Biología y Medicina Experimental (IBYME-CONICET), Buenos Aires, Argentina. Electronic address: gustavoh@ibyme.conicet.gov.ar.
Roger Castells-GraellsDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, California, Los Angeles (UCLA), Los Angeles, CA 90095, USA. Electronic address: rcastells@cnio.es.
Jose A RodriguezDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, California, Los Angeles (UCLA), Los Angeles, CA 90095, USA. Electronic address: jrodriguez@mbi.ucla.edu.

Funding

NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9M
NCCAT: National Center for CryoEM Access and TrainingR24GM154192 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI EDWARD T ENG, Jeffrey S Kieft · 2024 to 2026
$21.0M
Research Training in Cell and Molecular BiologyT32GM145388 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Jorge Torres · 2022 to 2026
$5.2M
Micro Electron Diffraction of Toxic and/or Infectious Macromolecular NanoassembliesR35GM128867 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Jose Alfonso Rodriguez · 2018 to 2026
$3.1M
NIAID NIH HHS HHSN272201700041INIGMS NIH HHS R24 GM154192NIGMS NIH HHS R35 GM128867NIGMS NIH HHS T32 GM145388NIGMS NIH HHS U24 GM129539
6 · The paper itself

Abstract

A transmembrane glycoprotein complex (GPC) decorates the Junin mammarenavirus (JUNV) that causes New World hemorrhagic fevers. We leveraged single-particle cryoelectron microscopy (cryo-EM) to image the full-length JUNV GPC directly on pseudotyped virus (PV) membranes and bound by two JUNV-neutralizing antibodies: Candid#1 vaccine-elicited CR1-28 and J199, a potent therapeutic against Argentine hemorrhagic fever (AHF). The 3.8 Å resolution in situ structures of the antibody-neutralized, 3-fold symmetric JUNV GPC reveal its ectodomain architecture, signal peptide-bound transmembrane region, zinc-binding luminal domain, and post-translational modifications. JUNV-GPC sequence variants highlight the functional importance of the signal peptide transmembrane helix register for virus infection and attenuating Candid#1-associated variants. Overlapping CR1-28 and J199 epitopes suggest a common receptor-blocking mechanism for JUNV neutralization, while a J199-induced, symmetric GPC reorientation may further drive its potent inhibition of JUNV lethality in mice, compared to receptor blockade alone. This underscores the utility of in situ insights into GPC function and neutralization.

Indexed as

Antibodies, NeutralizingAntibodies, ViralGlycoproteinsJunin virusAnimalsCryoelectron MicroscopyEpitopesHemorrhagic Fever, AmericanHumansMiceAntibodies, NeutralizingAntibodies, ViralEpitopesGlycoproteinsantiviralarenavirus membraneCP: ImmunologyCP: Microbiologyglycoproteinin situ cryo-EMneutralizing antibody

Identifiers

PMID40632652
PMCPMC12450071

What OpenQuestion holds

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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.