Evidence map›Paper›PMID 33572517›Full record

ArticleViruses2021

Potential Dual Role of West Nile Virus NS2B in Orchestrating NS3 Enzymatic Activity in Viral Replication.

Alanna C Tseng, Vivek R Nerurkar, Kabi R Neupane, Helmut Kae, Pakieli H Kaufusi

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 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. West Nile virus unmasked: from gene variability to future challenges.Frontiers in cellular and infection microbiology · 2025
    Review
  3. Article
  4. Article
  5. Development of Antibody-Based Therapeutics Against West Nile Virus in Plants.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. 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

5 authors at 1 institution in 1 country.

Alanna C TsengDepartment of Tropical Medicine, Medical Microbiology and Pharmacology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96813, USA.
Vivek R NerurkarDepartment of Tropical Medicine, Medical Microbiology and Pharmacology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96813, USA.ORCID 0000-0002-2044-2784
Kabi R NeupaneDivision of Math and Sciences, Leeward Community College, University of Hawaii, Pearl City, HI 96782, USA.
Helmut KaeDivision of Math and Sciences, Leeward Community College, University of Hawaii, Pearl City, HI 96782, USA.
Pakieli H KaufusiDepartment of Tropical Medicine, Medical Microbiology and Pharmacology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96813, USA.
University of Hawaiʻi at Mānoa · US

Funding

UH Hilo COP A&RP20GM103466 · NIGMS · UNIVERSITY OF HAWAII AT MANOA · PI Peter R Hoffmann · 2012 to 2026
$60.3M
Small Grants ProgramP30GM114737 · NIGMS · UNIVERSITY OF HAWAII AT MANOA · PI NERURKAR, VIVEK RAMCHANDRA · 2015 to 2022
$8.1M
NIGMS NIH HHS P20 GM103466NIGMS NIH HHS P30 GM114737
6 · The paper itself

Abstract

West Nile virus (WNV) nonstructural protein 3 (NS3) harbors the viral triphosphatase and helicase for viral RNA synthesis and, together with NS2B, constitutes the protease responsible for polyprotein processing. NS3 is a soluble protein, but it is localized to specialized compartments at the rough endoplasmic reticulum (RER), where its enzymatic functions are essential for virus replication. However, the mechanistic details behind the recruitment of NS3 from the cytoplasm to the RER have not yet been fully elucidated. In this study, we employed immunofluorescence and biochemical assays to demonstrate that NS3, when expressed individually and when cleaved from the viral polyprotein, is localized exclusively to the cytoplasm. Furthermore, NS3 appeared to be peripherally recruited to the RER and proteolytically active when NS2B was provided in trans. Thus, we provide evidence for a potential additional role for NS2B in not only serving as the cofactor for the NS3 protease, but also in recruiting NS3 from the cytoplasm to the RER for proper enzymatic activity. Results from our study suggest that targeting the interaction between NS2B and NS3 in disrupting the NS3 ER localization may be an attractive avenue for antiviral drug discovery.

Indexed as

Virus ReplicationCytoplasmDEAD-box RNA HelicasesEndoplasmic Reticulum, RoughHumansNucleoside-TriphosphataseProtein TransportRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesWest Nile FeverWest Nile virusDEAD-box RNA HelicasesNS2B protein, flavivirusNS3 protein, flavivirusNucleoside-TriphosphataseRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral Proteasesendoplasmic reticulumflavivirusmembrane structuresNS2BNS3West Nile Virus

Identifiers

PMID33572517
PMCPMC7911885
OpenAlexW3128634813

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.