Evidence map›Paper›PMID 42321170›Full record

ArticleNature communications2026

Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.

Aaron J May, Muralikrishna Lella, Jared Lindenberger, Alex Berkman, Ujjwal Kumar, Kejun Liu, Moumita Dutta, Maggie Barr, Rob Parks, Xiaozhi Lu and 25 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 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

5 · Who and what money

Authors and funding

35 authors.

Aaron J MayDuke Human Vaccine Institute, Duke University, Durham, NC, USA. aaron.may@duke.edu.ORCID http://orcid.org/0000-0003-2262-9750
Muralikrishna Lella *Duke Human Vaccine Institute, Duke University, Durham, NC, USA.
Jared Lindenberger *Duke Human Vaccine Institute, Duke University, Durham, NC, USA.
Alex Berkman *Duke Human Vaccine Institute, Duke University, Durham, NC, USA.
Ujjwal KumarDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Kejun LiuDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Moumita DuttaDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Maggie BarrDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Rob ParksDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Xiaozhi LuDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Madison BerryDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Amanda PowellDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Amelia G ThompsonVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Sravya Sowdamini NakkaNational Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.
Camila T FrançaNational Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.
Xiao HuangDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Arpita MrigwaniDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Kijun SongDuke Human Vaccine Institute, Duke University, Durham, NC, USA.ORCID http://orcid.org/0000-0002-6037-9345
Victor IlevbareDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Salam SammourDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Chan Soo ParkDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Radha Devkota AdhikariDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Priyanka DevkotaDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Katarzyna JanowskaDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Yanshun LiuDuke Human Vaccine Institute, Duke University, Durham, NC, USA.ORCID http://orcid.org/0009-0005-3634-4993
Garrett ScapellatoDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Taylor N SpenceDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Katayoun MansouriDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Kevin WieheDuke Human Vaccine Institute, Duke University, Durham, NC, USA.
Nancy J SullivanNational Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.
Rosemarie MasonVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Robert J EdwardsDuke Human Vaccine Institute, Duke University, Durham, NC, USA.ORCID http://orcid.org/0000-0003-4446-1194
Kevin O SaundersDuke Human Vaccine Institute, Duke University, Durham, NC, USA.ORCID http://orcid.org/0000-0001-7399-7954
Barton F HaynesDuke Human Vaccine Institute, Duke University, Durham, NC, USA.ORCID http://orcid.org/0000-0002-7643-9023
Priyamvada AcharyaDuke Human Vaccine Institute, Duke University, Durham, NC, USA. priyamvada.acharya@duke.edu.ORCID http://orcid.org/0000-0002-0089-277X

Funding

Structural characterization of Fab-dimerized glycan-reactive antibodies that neutralize HIV-1R01AI165147 · NIAID · DUKE UNIVERSITY · PI ACHARYA, PRIYAMVADA, WILLIAMS, WILTON B · 2021 to 2025
$3.4M
Data commons for 'omic, microscopy and analysis core facilitiesS10OD018164 · OD · DUKE UNIVERSITY · PI WRAY, GREGORY A. · 2014 to 2014
$598k
NIAID NIH HHS R01 AI165147NIH HHS S10 OD018164U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) AI 165147
6 · The paper itself

Abstract

Henipaviruses, in the Paramyxoviridae family, includes the highly virulent Nipah virus that causes reoccurring outbreaks of deadly disease. Recent discoveries of Henipavirus-like species, including the zoonotic Langya virus, have revealed much higher antigenic diversity than currently characterized and prompted the reorganization of these viruses into the Henipavirus and Parahenipavirus genera. Here, to explore the limits of structural and antigenic variation in both genera, collectively referred to as HNVs, we construct an expanded, diverse panel of HNV fusion and attachment glycoproteins from non-redundant HNV strains that better reflect global HNV diversity. We express and purify the fusion protein ectodomains and the attachment protein head domains and study their biochemical and biophysical properties. We perform immunization experiments in mice, eliciting antibodies reactive to multiple HNV fusion proteins. Cryo-electron microscopy structures elucidate molecular determinants of differential pre-fusion state stability and higher order contacts. A crystal structure of the Gamak virus attachment head domain reveals an additional domain appended to the conserved 6-bladed, β-propeller fold. Taken together, these studies expand the known structural and antigenic limits of the HNVs, reveal cross-reactive epitopes within both genera and provide foundational data for the development of broadly reactive countermeasures.

Indexed as

Antigens, ViralGlycoproteinsHenipavirusAnimalsAntibodies, ViralAntigenic VariationCryoelectron MicroscopyCrystallography, X-RayHenipavirus InfectionsHumansMiceViral Fusion ProteinsAntibodies, ViralAntigens, ViralGlycoproteinsViral Fusion Proteins

Identifiers

PMID42321170
PMCPMC13433794

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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.