Evidence map›Paper›PMID 31960795›Full record

ArticleeLife2020

A polyomavirus peptide binds to the capsid VP1 pore and has potent antiviral activity against BK and JC polyomaviruses.

Joshua R Kane, Susan Fong, Jacob Shaul, Alexandra Frommlet, Andreas O Frank, Mark Knapp, Dirksen E Bussiere, Peter Kim, Elizabeth Ornelas, Carlos Cuellar and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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

13 authors at 1 institution in 1 country.

Joshua R KaneInfectious Diseases, Novartis Institutes for BioMedical Research, Emeryville, United States.ORCID 0000-0002-6547-638X
Susan FongInfectious Diseases, Novartis Institutes for BioMedical Research, Emeryville, United States.
Jacob ShaulChemical Biology and Therapeutics, Novartis Institutes for BioMedical Research, Emeryville, United States.
Alexandra FrommletGlobal Discovery Chemistry, Novartis Institutes for BioMedical Research, Emeryville, United States.
Andreas O FrankGlobal Discovery Chemistry, Novartis Institutes for BioMedical Research, Emeryville, United States.
Mark KnappGlobal Discovery Chemistry, Novartis Institutes for BioMedical Research, Emeryville, United States.
Dirksen E BussiereGlobal Discovery Chemistry, Novartis Institutes for BioMedical Research, Emeryville, United States.
Peter KimInfectious Diseases, Novartis Institutes for BioMedical Research, Emeryville, United States.
Elizabeth OrnelasGlobal Discovery Chemistry, Novartis Institutes for BioMedical Research, Emeryville, United States.
Carlos CuellarGlobal Discovery Chemistry, Novartis Institutes for BioMedical Research, Emeryville, United States.
Anastasia HyrinaChemical Biology and Therapeutics, Novartis Institutes for BioMedical Research, Emeryville, United States.
Johanna R AbendInfectious Diseases, Novartis Institutes for BioMedical Research, Emeryville, United States.
Charles A WartchowGlobal Discovery Chemistry, Novartis Institutes for BioMedical Research, Emeryville, United States.ORCID 0000-0002-0123-1455
Novartis (United States) · US

Funding

Novartis Postdoctoral fellowship
6 · The paper itself

Abstract

In pursuit of therapeutics for human polyomaviruses, we identified a peptide derived from the BK polyomavirus (BKV) minor structural proteins VP2/3 that is a potent inhibitor of BKV infection with no observable cellular toxicity. The thirteen-residue peptide binds to major structural protein VP1 with single-digit nanomolar affinity. Alanine-scanning of the peptide identified three key residues, substitution of each of which results in ~1000 fold loss of binding affinity with a concomitant reduction in antiviral activity. Structural studies demonstrate specific binding of the peptide to the pore of pentameric VP1. Cell-based assays demonstrate nanomolar inhibition (EC

Indexed as

BK VirusAntiviral AgentsCapsid ProteinsCells, CulturedHEK293 CellsHumansJC VirusPeptidesProtein BindingAntiviral AgentsCapsid ProteinsPeptidesVP1 protein, polyomavirusantiviralbiochemistryBK polyomaviruschemical biologyhumaninfectious diseaseJC polyomavirusmicrobiologypeptide

Identifiers

PMID31960795
PMCPMC6974358
OpenAlexW2999912061

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.