Evidence map›Paper›PMID 41528847›Full record

ArticleCell reports2026

Cryo-EM structures of antibodies elicited by germline-targeting HIV MPER epitope scaffolds.

Jiachen Huang, Olivia M Swanson, Kimmo Rantalainen, Monica L Fernández-Quintero, Johannes R Loeffler, Ryan Tingle, Erik Georgeson, Nicole Phelps, Gabriel Ozorowski, Torben Schiffner and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Jiachen HuangDepartment of Integrative Structural and Computational Biology, the Scripps Research Institute, La Jolla, CA, USA.
Olivia M SwansonDepartment of Integrative Structural and Computational Biology, the Scripps Research Institute, La Jolla, CA, USA; Department of Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA.
Kimmo RantalainenDepartment of Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA.
Monica L Fernández-QuinteroDepartment of Integrative Structural and Computational Biology, the Scripps Research Institute, La Jolla, CA, USA.
Johannes R LoefflerDepartment of Integrative Structural and Computational Biology, the Scripps Research Institute, La Jolla, CA, USA.
Ryan TingleDepartment of Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA.
Erik GeorgesonDepartment of Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA.
Nicole PhelpsDepartment of Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA.
Gabriel OzorowskiDepartment of Integrative Structural and Computational Biology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA.
Torben SchiffnerDepartment of Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA.
William R SchiefDepartment of Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA; Moderna, Inc., Cambridge, MA, USA. Electronic address: schief@scripps.edu.
Andrew B WardDepartment of Integrative Structural and Computational Biology, the Scripps Research Institute, La Jolla, CA, USA; Consortia for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVD), the Scripps Research Institute, La Jolla, CA, USA; IAVI Neutralizing Antibody Center, the Scripps Research Institute, La Jolla, CA, USA. Electronic address: andrew@scripps.edu.

Funding

Development of soluble and membrane bound immunogens to shepherd HIV-1 MPER specific BCR maturationF31AI179426 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI Olivia Swanson · 2024 to 2026
$107k
NIAID NIH HHS F31 AI179426
6 · The paper itself

Abstract

Applying cryoelectron microscopy (cryo-EM) to small protein complexes is usually challenging due to their lack of features for particle alignment. Here, we characterized antibody responses to 21 kDa human immunodeficiency virus (HIV) membrane-proximal external region germline-targeting (MPER-GT) immunogens through cryo-EM by complexing them with 10E8 or Fabs derived from MPER-GT-immunized animals. Distinct antibody-antigen interactions were analyzed using atomic models generated from cryo-EM maps. Mutagenesis screening revealed that off-target monoclonal antibodies (mAbs), which do not compete with 10E8, bind non-MPER epitopes, and the binding of two most dominant epitopes were verified by cryo-EM. The structures of 10E8-class on-target Fabs showed binding patterns that resemble the YxFW motif in the 10E8 heavy chain complementarity-determining region 3 (HCDR3) loop. Additionally, we demonstrate that high-resolution maps can be generated from heterogeneous samples with pooled competing Fabs. Overall, our findings will facilitate the optimization of MPER-GT antigens and push the size limit for cryo-EM-based epitope mapping with smaller antigens and heterogeneous antibody mixes.

Indexed as

Cryoelectron MicroscopyEpitopesGerm CellsHIV-1HIV AntibodiesHIV Envelope Protein gp41AnimalsAntibodies, MonoclonalHumansImmunoglobulin Fab FragmentsModels, MolecularAntibodies, MonoclonalEpitopesHIV AntibodiesHIV Envelope Protein gp41Immunoglobulin Fab FragmentsCP: immunologyCP: molecular biologycryo-EMgermline targetingHIV-1 Envmembrane-proximal external regionMPER

Identifiers

PMID41528847
PMCPMC13335052

What Socratic 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 Socratic graph.