Evidence map›Paper›PMID 36853802›Full record

ArticleJCI insight2023

Potently neutralizing human mAbs against the zoonotic pararubulavirus Sosuga virus.

Helen M Parrington, Nurgun Kose, Erica Armstrong, Laura Handal, Summer Diaz, Joseph Reidy, Jinhui Dong, Guillaume Be Stewart-Jones, Punya Shrivastava-Ranjan, Shilpi Jain and 3 more

Open access · goldAbstract read
In one paragraph

Article in JCI insight, 2023. 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
0.2field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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 3 institutions in 3 countries.

Helen M ParringtonDepartment of Pathology, Microbiology and Immunology.
Nurgun KoseVanderbilt Vaccine Center, and Department of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Erica ArmstrongVanderbilt Vaccine Center, and Department of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Laura HandalVanderbilt Vaccine Center, and Department of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Summer DiazVanderbilt Vaccine Center, and Department of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Joseph ReidyVanderbilt Vaccine Center, and Department of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Jinhui DongVanderbilt Vaccine Center, and Department of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Guillaume Be Stewart-JonesVaccine Research Center, NIH, Bethesda, Maryland, USA.
Punya Shrivastava-RanjanViral Special Pathogens Branch, Division of High Consequence Pathogens and Pathology, CDC, Atlanta, Georgia, USA.
Shilpi JainViral Special Pathogens Branch, Division of High Consequence Pathogens and Pathology, CDC, Atlanta, Georgia, USA.
César G AlbariñoViral Special Pathogens Branch, Division of High Consequence Pathogens and Pathology, CDC, Atlanta, Georgia, USA.
Robert H CarnahanVanderbilt Vaccine Center, and Department of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
James E CroweDepartment of Pathology, Microbiology and Immunology.
Vanderbilt University Medical Center · USCenters for Disease Control and Prevention · USBipar · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sosuga virus (SOSV) is a recently discovered paramyxovirus with a single known human case of disease. There has been little laboratory research on SOSV pathogenesis or immunity, and no approved therapeutics or vaccines are available. Here, we report the discovery of human mAbs from the circulating memory B cells of the only known human case and survivor of SOSV infection. We isolated 6 mAbs recognizing the functional attachment protein hemagglutinin-neuraminidase (HN) and 18 mAbs against the fusion (F) protein. The anti-HN mAbs all targeted the globular head of the HN protein and could be organized into 4 competition-binding groups that exhibited epitope diversity. The anti-F mAbs can be divided into pre- or postfusion conformation-specific categories and further into 8 competition-binding groups. The only Ab in the panel that did not display neutralization activity was the single postfusion-specific anti-F mAb. Most of the anti-HN mAbs were more potently neutralizing than the anti-F mAbs, with mAbs in 1 of the HN competition-binding groups possessing ultrapotent (<1 ng/mL) half-maximal inhibitory virus neutralization values. These findings provide insight into the molecular basis for human Ab recognition of paramyxovirus surface proteins and the mechanisms of SOSV neutralization.

Indexed as

Antibodies, MonoclonalParamyxoviridaeHumansViral ProteinsAntibodies, MonoclonalViral ProteinsAdaptive immunityImmunoglobulinsImmunologyInfectious disease

Identifiers

PMID36853802
PMCPMC10243738
OpenAlexW4322617510

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.