Evidence map›Paper›PMID 30996086›Full record

ArticleJournal of virology2019

Phosphorylation of Human Papillomavirus Type 16 L2 Contributes to Efficient Virus Infectious Entry.

Justyna Broniarczyk, Paola Massimi, David Pim, Martina Bergant Marušič, Michael P Myers, Robert L Garcea, Lawrence Banks

Open access · bronzeAbstract 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 13 citations in OpenAlex.

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  3. bioRxiv : the preprint server for biology · 2025
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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 4 institutions in 4 countries.

Justyna BroniarczykTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Paola MassimiTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
David PimTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Martina Bergant MarušičLaboratory for Environmental and Life Sciences, University of Nova Gorica, Nova Gorica, Slovenia.
Michael P MyersProtein Networks, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Robert L GarceaBioFrontiers Institute and the Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, USA.
Lawrence BanksTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy banks@icgeb.org.
International Centre for Genetic Engineering and Biotechnology · ITAdam Mickiewicz University in Poznań · PLUniversity of Colorado Boulder · USUniversity of Nova Gorica · SI

Funding

Treatment of HIV- and HIV+ Patients with HPV16+ CIN2/3 Using pNGLV4a-hCRTE6E7L2 DNA vaccine administered intramuscularly via electroporationP50CA098252 · NCI · JOHNS HOPKINS UNIVERSITY · PI TZYY-CHOOU WU · 2003 to 2026
$53.5M
MECHANISMS IN POLYOMA VIRUS ASSEMBLYR01CA037667 · NCI · UNIVERSITY OF COLORADO DENVER · PI GARCEA, ROBERT L · 1985 to 2018
$6.3M
NCI NIH HHS P50 CA098252NCI NIH HHS R01 CA037667
6 · The paper itself

Abstract

The human papillomavirus (HPV) capsid comprises two viral proteins, L1 and L2, with the L2 component being essential to ensure efficient endocytic transport of incoming viral genomes. Several studies have previously reported that L1 and L2 are posttranslationally modified, but it is uncertain whether these modifications affect HPV infectious entry. Using a proteomic screen, we identified a highly conserved phospho-acceptor site on the HPV-16 and bovine papillomavirus 1 (BPV-1) L2 proteins. The phospho-modification of L2 and its presence in HPV pseudovirions (PsVs) were confirmed using anti-phospho-L2-specific antibodies. Mutation of the phospho-acceptor sites of both HPV-16 and BPV-1 L2 resulted in the production of infectious virus particles, with no differences in efficiencies of packaging the reporter DNA. However, these mutated PsVs showed marked defects in infectious entry. Further analysis revealed a defect in uncoating, characterized by a delay in the exposure of a conformational epitope on L1 that indicates capsid uncoating. This uncoating defect was accompanied by a delay in the proteolysis of both L1 and L2 in mutated HPV-16 PsVs. Taken together, these studies indicate that phosphorylation of L2 during virus assembly plays an important role in optimal uncoating of virions during infection, suggesting that phosphorylation of the viral capsid proteins contributes to infectious entry.

Indexed as

Virus InternalizationBovine papillomavirus 1Capsid ProteinsCell LineEpitopesGenome, ViralHuman papillomavirus 16HumansMutationOncogene Proteins, ViralPapillomavirus InfectionsPhosphorylationProtein ConformationProteomicsViral ProteinsVirionCapsid ProteinsEpitopesL1 protein, Human papillomavirus type 16L2 protein, Human papillomavirus type 16Oncogene Proteins, ViralViral ProteinsHPVinfectionL2protein phosphorylation

Identifiers

PMID30996086
PMCPMC6580975
OpenAlexW2950295045

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.