Evidence map›Paper›PMID 32535702›Full record

ArticleMedical microbiology and immunology2020

HPV caught in the tetraspanin web?

Jérôme Finke, Lisa Hitschler, Klaus Boller, Luise Florin, Thorsten Lang

Open access · hybridAbstract read
In one paragraph

Article in Medical microbiology and immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Functional analysis ofThe Journal of general virology · 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

5 authors at 3 institutions in 1 country.

Jérôme FinkeDepartment of Membrane Biochemistry, Life & Medical Sciences (LIMES) Institute, University of Bonn, Carl-Troll-Straße 31, 53115, Bonn, Germany. s6jefink@uni-bonn.de.ORCID http://orcid.org/0000-0001-9528-5763
Lisa HitschlerDepartment of Membrane Biochemistry, Life & Medical Sciences (LIMES) Institute, University of Bonn, Carl-Troll-Straße 31, 53115, Bonn, Germany.
Klaus BollerPaul Ehrlich Institute, Paul-Ehrlich-Straße 51-59, 63225, Langen, Germany.
Luise FlorinInstitute for Virology and Research Center for Immunotherapy (FZI), University Medical Centre of the Johannes Gutenberg University Mainz, Obere Zahlbacher Straße 67, 55131, Mainz, Germany.
Thorsten LangDepartment of Membrane Biochemistry, Life & Medical Sciences (LIMES) Institute, University of Bonn, Carl-Troll-Straße 31, 53115, Bonn, Germany. thorsten.lang@uni-bonn.de.
University of Bonn · DEJohannes Gutenberg University Mainz · DEPaul Ehrlich Institut · DE

Funding

Deutsche Forschungsgemeinschaft FL 696/3-1Deutsche Forschungsgemeinschaft LA 1272/8-1
6 · The paper itself

Abstract

Tetraspanins are master organizers of the cell membrane. Recent evidence suggests that tetraspanins themselves may become crowded by virus particles and that these crowds/aggregates co-internalize with the viral particles. Using microscopy, we studied human papillomavirus (HPV) type 16-dependent aggregates on the cell surface of tetraspanin overexpressing keratinocytes. We find that aggregates are (1) rich in at least two different tetraspanins, (2) three-dimensional architectures extending up to several micrometers into the cell, and (3) decorated intracellularly by filamentous actin. Moreover, in cells not overexpressing tetraspanins, we note that obscurin-like protein 1 (OBSL1), which is thought to be a cytoskeletal adaptor, associates with filamentous actin. We speculate that HPV contact with the cell membrane could trigger the formation of a large tetraspanin web. This web may couple the virus contact site to the intracellular endocytic actin machinery, possibly involving the cytoskeletal adaptor protein OBSL1. Functionally, such a tetraspanin web could serve as a virus entry platform, which is co-internalized with the virus particle.

Indexed as

ActinsCytoskeletal ProteinsEndocytosisHaCaT CellsHeLa CellsHep G2 CellsHuman papillomavirus 16HumansMicroscopy, ConfocalMicroscopy, ElectronPapillomavirus InfectionsPlakinsTetraspanin 24Tetraspanin 30VirionVirus InternalizationActinsCytoskeletal ProteinsOBSL1 protein, humanPlakinsTetraspanin 24Tetraspanin 30ActinCD151CD63MicrodomainsOBSL1PapillomavirusPathogen endocytosisProtein nanoclustering

Identifiers

PMID32535702
PMCPMC7293171
OpenAlexW3035439768

What OpenQuestion holds

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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.