Evidence map›Paper›PMID 33085724›Full record

ArticlePLoS pathogens2020

p120 catenin recruits HPV to γ-secretase to promote virus infection.

Mara Calypso Harwood, Allison Jade Dupzyk, Takamasa Inoue, Daniel DiMaio, Billy Tsai

Abstract read
In one paragraph

Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Human Papilloma Virus-Infected Cells.Sub-cellular biochemistry · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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

5 authors.

Mara Calypso HarwoodDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI, United States of America.ORCID 0000-0003-4976-8400
Allison Jade DupzykDepartment of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA, United States of America.ORCID 0000-0003-1473-4489
Takamasa InouePathogen Research Section, Central Research Laboratory, Research and Development Division, Japan Blood Products Organization, Kobe, Japan.
Daniel DiMaioDepartment of Genetics, Yale School of Medicine, New Haven, CT, United States of America.
Billy TsaiDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI, United States of America.ORCID 0000-0003-2859-1415

Funding

CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
Transport of polyomavirus across the ER membraneR01AI064296 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TSAI, BILLY · 2006 to 2021
$5.5M
Retrograde TGN/Golgi transport and nuclear targeting of HPV during entryR01AI150897 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Daniel C. Dimaio, Billy Tsai · 2020 to 2026
$3.5M
Investigating novel host factors promoting human papillomavirus infectionF31AI152365 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI HARWOOD, MARA CALYPSO · 2021 to 2023
$97k
NIAID NIH HHS F31 AI152365NIAID NIH HHS R01 AI064296NIAID NIH HHS R01 AI150897NIGMS NIH HHS T32 GM007315
6 · The paper itself

Abstract

During internalization and trafficking, human papillomavirus (HPV) moves from the cell surface to the endosome where the transmembrane protease γ-secretase promotes insertion of the viral L2 capsid protein into the endosome membrane. Protrusion of L2 through the endosome membrane into the cytosol allows the recruitment of cytosolic host factors that target the virus to the Golgi en route for productive infection. How endosome-localized HPV is delivered to γ-secretase, a decisive infection step, is unclear. Here we demonstrate that cytosolic p120 catenin, likely via an unidentified transmembrane protein, interacts with HPV at early time-points during viral internalization and trafficking. In the endosome, p120 is not required for low pH-dependent disassembly of the HPV L1 capsid protein from the incoming virion. Rather, p120 is required for HPV to interact with γ-secretase-an interaction that ensures the virus is transported along a productive route. Our findings clarify an enigmatic HPV infection step and provide critical insights into HPV infection that may lead to new therapeutic strategies against HPV-induced diseases.

Indexed as

Virus InternalizationAlphapapillomavirusAmyloid Precursor Protein SecretasesCapsid ProteinsCateninsEndosomesHeLa CellsHumansIntracellular MembranesOncogene Proteins, ViralPapillomavirus InfectionsProtein TransportVirionAmyloid Precursor Protein SecretasesCapsid ProteinsCateninsHPV L1 protein, Human papillomavirusOncogene Proteins, Viral

Identifiers

PMID33085724
PMCPMC7577436

What OpenQuestion holds

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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.