Evidence map›Paper›PMID 33804519›Full record

ArticleViruses2021

Isolation and Characterization of Cross-Reactive Human Monoclonal Antibodies That Potently Neutralize Australian Bat Lyssavirus Variants and Other Phylogroup 1 Lyssaviruses.

Dawn L Weir, Si'Ana A Coggins, Bang K Vu, Jessica Coertse, Lianying Yan, Ina L Smith, Eric D Laing, Wanda Markotter, Christopher C Broder, Brian C Schaefer

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 9 citations in OpenAlex.

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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

10 authors at 5 institutions in 3 countries.

Dawn L WeirDepartment of Microbiology, Uniformed Services University, Bethesda, MD 20814, USA.
Si'Ana A CogginsDepartment of Microbiology, Uniformed Services University, Bethesda, MD 20814, USA.
Bang K VuDepartment of Microbiology, Uniformed Services University, Bethesda, MD 20814, USA.
Jessica CoertseDepartment of Medical Virology, Faculty of Health Sciences, University of Pretoria, Pretoria, Gauteng 0001, South Africa.ORCID 0000-0002-8376-6508
Lianying YanDepartment of Microbiology, Uniformed Services University, Bethesda, MD 20814, USA.
Ina L SmithRisk Evaluation and Preparedness Program, Health and Biosecurity, CSIRO, Black Mountain, Australian Capital Territory 2601, Canberra, ACT 2601, Australia.
Eric D LaingDepartment of Microbiology, Uniformed Services University, Bethesda, MD 20814, USA.
Wanda MarkotterDepartment of Medical Virology, Faculty of Health Sciences, University of Pretoria, Pretoria, Gauteng 0001, South Africa.ORCID 0000-0002-7550-0080
Christopher C BroderDepartment of Microbiology, Uniformed Services University, Bethesda, MD 20814, USA.ORCID 0000-0001-5382-0510
Brian C SchaeferDepartment of Microbiology, Uniformed Services University, Bethesda, MD 20814, USA.ORCID 0000-0001-8877-3507
Uniformed Services University of the Health Sciences · USHenry M. Jackson Foundation · USCSIRO Health and Biosecurity · AUNational Health Laboratory Service · ZAUniversity of Pretoria · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Australian bat lyssavirus (ABLV) is a rhabdovirus that circulates in four species of pteropid bats (ABLVp) and the yellow-bellied sheath-tailed bat (ABLVs) in mainland Australia. In the three confirmed human cases of ABLV, rabies illness preceded fatality. As with rabies virus (RABV), post-exposure prophylaxis (PEP) for potential ABLV infections consists of wound cleansing, administration of the rabies vaccine and injection of rabies immunoglobulin (RIG) proximal to the wound. Despite the efficacy of PEP, the inaccessibility of human RIG (HRIG) in the developing world and the high immunogenicity of equine RIG (ERIG) has led to consideration of human monoclonal antibodies (hmAbs) as a passive immunization option that offers enhanced safety and specificity. Using a recombinant vesicular stomatitis virus (rVSV) expressing the glycoprotein (G) protein of ABLVs and phage display, we identified two hmAbs, A6 and F11, which completely neutralize ABLVs/ABLVp, and RABV at concentrations ranging from 0.39 and 6.25 µg/mL and 0.19 and 0.39 µg/mL respectively. A6 and F11 recognize overlapping epitopes in the lyssavirus G protein, effectively neutralizing phylogroup 1 lyssaviruses, while having little effect on phylogroup 2 and non-grouped diverse lyssaviruses. These results suggest that A6 and F11 could be effective therapeutic and diagnostic tools for phylogroup 1 lyssavirus infections.

Indexed as

PhylogenyAnimalsAntibodies, MonoclonalAntibodies, ViralAustraliaBites and StingsCell Surface Display TechniquesChiropteraCross ReactionsEpitopesHEK293 CellsHorsesHumansLyssavirusNeutralization TestsPost-Exposure ProphylaxisAntibodies, MonoclonalAntibodies, ViralEpitopesRabies VaccinesABLVbatglycoproteinlyssavirusesmonoclonal antibodiesneutralizationphage displayrabiesRABV

Identifiers

PMID33804519
PMCPMC8001737
OpenAlexW3128868990

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.