Evidence map›Paper›PMID 30232190›Full record

ArticleJournal of virology2018

Characterization of Antibody Interactions with the G Protein of Vesicular Stomatitis Virus Indiana Strain and Other Vesiculovirus G Proteins.

Altar M Munis, Maha Tijani, Mark Hassall, Giada Mattiuzzo, Mary K Collins, Yasuhiro Takeuchi

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

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  15. Lentivector Producer Cell Lines with Stably Expressed Vesiculovirus Envelopes.Molecular therapy. Methods & clinical development · 2018
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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

6 authors at 3 institutions in 2 countries.

Altar M MunisDivision of Advanced Therapies, National Institute for Biological Standards and Control, South Mimms, United Kingdom.
Maha TijaniDivision of Advanced Therapies, National Institute for Biological Standards and Control, South Mimms, United Kingdom.
Mark HassallDivision of Virology, National Institute for Biological Standards and Control, South Mimms, United Kingdom.
Giada MattiuzzoDivision of Virology, National Institute for Biological Standards and Control, South Mimms, United Kingdom.
Mary K CollinsDivision of Advanced Therapies, National Institute for Biological Standards and Control, South Mimms, United Kingdom.
Yasuhiro TakeuchiDivision of Advanced Therapies, National Institute for Biological Standards and Control, South Mimms, United Kingdom y.takeuchi@ucl.ac.uk.
National Institute for Biological Standards and Control · GBUniversity College London · GBOkinawa Institute of Science and Technology Graduate University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vesicular stomatitis virus Indiana strain G protein (VSVind.G) is the most commonly used envelope glycoprotein to pseudotype lentiviral vectors (LV) for experimental and clinical applications. Recently, G proteins derived from other vesiculoviruses (VesG), for example, Cocal virus, have been proposed as alternative LV envelopes with possible advantages over VSVind.G. Well-characterized antibodies that recognize VesG will be useful for vesiculovirus research, development of G protein-containing advanced therapy medicinal products (ATMPs), and deployment of VSVind-based vaccine vectors. Here, we show that one commercially available monoclonal antibody, 8G5F11, binds to and neutralizes G proteins from three strains of VSV, as well as Cocal and Maraba viruses, whereas the other commercially available monoclonal anti-VSVind.G antibody, IE9F9, binds to and neutralizes only VSVind.G. Using a combination of G protein chimeras and site-directed mutations, we mapped the binding epitopes of IE9F9 and 8G5F11 on VSVind.G. IE9F9 binds close to the receptor binding site and competes with soluble low-density lipoprotein receptor (LDLR) for binding to VSVind.G, explaining its mechanism of neutralization. In contrast, 8G5F11 binds close to a region known to undergo conformational changes when the G protein moves to its postfusion structure, and we propose that 8G5F11 cross-neutralizes VesGs by inhibiting this.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalAntibodies, NeutralizingAntigens, ViralCross ReactionsEpitopesHEK293 CellsHumansMembrane GlycoproteinsNeutralization TestsPhylogenySequence HomologyVesicular StomatitisVesicular stomatitis Indiana virusViral Envelope ProteinsAntibodies, MonoclonalAntibodies, NeutralizingAntigens, ViralEpitopesG protein, vesicular stomatitis virusMembrane GlycoproteinsViral Envelope Proteinsmonoclonal antibodiesneutralizing antibodiesvesiculovirusVSV

Identifiers

PMID30232190
PMCPMC6232470
OpenAlexW2949281755

What OpenQuestion holds

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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.