Evidence map›Paper›PMID 32295921›Full record

ArticleJournal of virology2020

Impairment of the DeISGylation Activity of Foot-and-Mouth Disease Virus Lpro Causes Attenuation

Gisselle N Medina, Paul Azzinaro, Elizabeth Ramirez-Medina, Joseph Gutkoska, Ying Fang, Fayna Diaz-San Segundo, Teresa de Los Santos

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 29 citations in OpenAlex.

  1. Kinetics of antiviral gene expression in foot-and-mouth disease virus serotype O infected BHK-21 cells.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025
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  9. An expanded lexicon for the ubiquitin code.Nature reviews. Molecular cell biology · 2023
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  15. Mutation of FMDV LFrontiers in veterinary science · 2022
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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 2 institutions in 1 country.

Gisselle N MedinaPlum Island Animal Disease Center (PIADC), ARS, USDA, Greenport, New York, USA gisselle.medina@ars.usda.gov teresa.delossantos@ars.usda.gov.
Paul AzzinaroPlum Island Animal Disease Center (PIADC), ARS, USDA, Greenport, New York, USA.
Elizabeth Ramirez-MedinaPlum Island Animal Disease Center (PIADC), ARS, USDA, Greenport, New York, USA.
Joseph GutkoskaPlum Island Animal Disease Center (PIADC), ARS, USDA, Greenport, New York, USA.
Ying FangKansas State University College of Veterinary Medicine, Manhattan, Kansas, USA.
Fayna Diaz-San SegundoPlum Island Animal Disease Center (PIADC), ARS, USDA, Greenport, New York, USA.
Teresa de Los SantosPlum Island Animal Disease Center (PIADC), ARS, USDA, Greenport, New York, USA gisselle.medina@ars.usda.gov teresa.delossantos@ars.usda.gov.
Plum Island Animal Disease Center · USKansas State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) affects several pathways of the host innate immune response. Previous studies in bovine cells demonstrated that deletions (leaderless [LLV]) or point mutations in Lpro result in increased expression of interferon (IFN) and IFN-stimulated genes (ISGs), including, among others, the ubiquitin-like protein modifier ISG15 and the ubiquitin specific peptidase USP18. In addition to its conventional papain-like protease activity, Lpro acts as a deubiquitinase (DUB) and deISGylase. In this study, we identified a conserved residue in Lpro that is involved in its interaction with ISG15. Mutation W105A rendered

Indexed as

AnimalsAntiviral AgentsCell LineCytokinesEndopeptidasesFemaleFoot-and-Mouth DiseaseFoot-and-Mouth Disease VirusHEK293 CellsHumansImmunity, InnateInterferon Type IMembrane ProteinsMiceMice, Inbred C57BLProteolysisAntiviral AgentsCytokinesEndopeptidasesInterferon Type IISG15 protein, humanleader proteinase, foot-and-mouth disease virusMembrane ProteinsSerine Endopeptidasestype I signal peptidaseUbiquitinsVaccines, AttenuateddeISGylationdeubiquitinationfoot-and-mouth disease virusinterferonsISG15ISGylationleaderpicornavirusPLPproteases

Identifiers

PMID32295921
PMCPMC7307143
OpenAlexW3016275689

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.