Evidence map›Paper›PMID 31511387›Full record

ArticleJournal of virology2019

Deep Mutational Scanning Comprehensively Maps How Zika Envelope Protein Mutations Affect Viral Growth and Antibody Escape.

Marion Sourisseau, Daniel J P Lawrence, Megan C Schwarz, Carina H Storrs, Ethan C Veit, Jesse D Bloom, Matthew J Evans

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 45 citations in OpenAlex.

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  16. popDMS infers mutation effects from deep mutational scanning data.bioRxiv : the preprint server for biology · 2024
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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

7 authors at 3 institutions in 1 country.

Marion Sourisseau *Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
Daniel J P Lawrence *Basic Sciences Division and Computational Biology Program, Fred Hutchinson Cancer Research Center, Seattle, Washington, USA.ORCID 0000-0002-2181-9352
Megan C SchwarzDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
Carina H StorrsDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
Ethan C VeitDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
Jesse D BloomBasic Sciences Division and Computational Biology Program, Fred Hutchinson Cancer Research Center, Seattle, Washington, USA jbloom@fredhutch.org matthew.evans@mssm.edu.ORCID 0000-0003-1267-3408
Matthew J EvansDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA jbloom@fredhutch.org matthew.evans@mssm.edu.ORCID 0000-0002-4991-3877
Icahn School of Medicine at Mount Sinai · USHoward Hughes Medical Institute · USUniversity of Washington · US

Funding

Prospectively characterizing the functional and antigenic effects of mutations to viral entry proteinsR01AI141707 · NIAID · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BLOOM, JESSE D · 2018 to 2022
$2.1M
FHCRC High-Performance Computing ClusterS10OD020069 · OD · FRED HUTCHINSON CANCER RESEARCH CENTER · PI KOOPERBERG, CHARLES L · 2015 to 2015
$600k
Deep mutational scanning of the Zika envelope proteinR21AI133649 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI EVANS, MATTHEW J · 2017 to 2018
$489k
Interplay between flaviviruses and lipidsR21AI140196 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI EVANS, MATTHEW J · 2019 to 2020
$480k
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI141707NIAID NIH HHS R21 AI133649NIAID NIH HHS R21 AI140196NIH HHS S10 OD020069
6 · The paper itself

Abstract

Functional constraints on viral proteins are often assessed by examining sequence conservation among natural strains, but this approach is relatively ineffective for Zika virus because all known sequences are highly similar. Here, we take an alternative approach to map functional constraints on Zika virus's envelope (E) protein by using deep mutational scanning to measure how all amino acid mutations to the E protein affect viral growth in cell culture. The resulting sequence-function map is consistent with existing knowledge about E protein structure and function but also provides insight into mutation-level constraints in many regions of the protein that have not been well characterized in prior functional work. In addition, we extend our approach to completely map how mutations affect viral neutralization by two monoclonal antibodies, thereby precisely defining their functional epitopes. Overall, our study provides a valuable resource for understanding the effects of mutations to this important viral protein and also offers a roadmap for future work to map functional and antigenic selection to Zika virus at high resolution.

Indexed as

MutationAmino Acid SequenceAnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralChlorocebus aethiopsEpitopesGlycoproteinsHEK293 CellsHigh-Throughput Nucleotide SequencingHumansImmune EvasionModels, MolecularProtein ConformationSequence AlignmentAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesglycoprotein E, FlavivirusGlycoproteinsViral Envelope Proteinsglycoproteinsmutagenesisneutralizing antibodiesvirus entryZika virus

Identifiers

PMID31511387
PMCPMC6854493
OpenAlexW2973042438

What OpenQuestion holds

Textmetadata
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.