Evidence map›Paper›PMID 30122350›Full record

ArticleCell2018

Cell-Penetrating Peptide Mediates Intracellular Membrane Passage of Human Papillomavirus L2 Protein to Trigger Retrograde Trafficking.

Pengwei Zhang, Gabriel Monteiro da Silva, Catherine Deatherage, Christopher Burd, Daniel DiMaio

Abstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed.

  1. Article
  2. Cargo-Adaptor Cooperation Programs Retromer Coat Architecture.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. The Rab5 effector Rabankyrin-5 mediates endosomal fusion and trafficking of human papillomavirus during early entry.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. γ-secretase facilitates retromer-mediated retrograde transport.bioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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.

Pengwei ZhangDepartment of Genetics, Yale School of Medicine, New Haven, CT 06520-8005, USA.
Gabriel Monteiro da SilvaDepartment of Genetics, Yale School of Medicine, New Haven, CT 06520-8005, USA.
Catherine DeatherageDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520-8002, USA.
Christopher BurdDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520-8002, USA.
Daniel DiMaioDepartment of Genetics, Yale School of Medicine, New Haven, CT 06520-8005, USA; Department of Therapeutic Radiology, Yale School of Medicine, New Haven, CT 06520-8040, USA; Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520-8024, USA; Yale Cancer Center, New Haven, CT 06520-8028, USA. Electronic address: daniel.dimaio@yale.edu.

Funding

VIRAL SMALL RNPS--ROLES IN CELL TRANSFORMATIONP01CA016038 · NCI · YALE UNIVERSITY · PI DIMAIO, DANIEL C. · 1985 to 2020
$25.6M
TRAFFICKING BY FYVE DOMAIN EFFECTORS OF PI3 KINASER01GM061221 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2000 to 2016
$5.2M
Role of Retromer-mediated Retrograde Transport in HPV EntryR01AI102876 · NIAID · YALE UNIVERSITY · PI DIMAIO, DANIEL C. · 2013 to 2020
$3.1M
Sorting and Trafficking in the Endosomal SystemR37GM061221 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2017 to 2021
$2.0M
NCI NIH HHS P01 CA016038NIAID NIH HHS R01 AI102876NIGMS NIH HHS R01 GM061221NIGMS NIH HHS R37 GM061221
6 · The paper itself

Abstract

Cell-penetrating peptides (CPPs) are short protein segments that can transport cargos into cells. Although CPPs are widely studied as potential drug delivery tools, their role in normal cell physiology is poorly understood. Early during infection, the L2 capsid protein of human papillomaviruses binds retromer, a cytoplasmic trafficking factor required for delivery of the incoming non-enveloped virus into the retrograde transport pathway. Here, we show that the C terminus of HPV L2 proteins contains a conserved cationic CPP that drives passage of a segment of the L2 protein through the endosomal membrane into the cytoplasm, where it binds retromer, thereby sorting the virus into the retrograde pathway for transport to the trans-Golgi network. These experiments define the cell-autonomous biological role of a CPP in its natural context and reveal how a luminal viral protein engages an essential cytoplasmic entry factor.

Indexed as

Amino Acid SequenceCapsid ProteinsCell-Penetrating PeptidesEndosomesGolgi ApparatusGreen Fluorescent ProteinsHEK293 CellsHeLa CellsHuman papillomavirus 16HumansMutagenesisOncogene Proteins, ViralProtein TransportRecombinant Fusion ProteinsSequence AlignmentVirus AttachmentCapsid ProteinsCell-Penetrating PeptidesGreen Fluorescent ProteinsL2 protein, Human papillomavirus type 16Oncogene Proteins, ViralRecombinant Fusion Proteinscell-penetrating peptideHIV TatHPVprotein transduction domainproximity ligation assayretrograderetromersplit GFPvirus

Identifiers

PMID30122350
PMCPMC6128760

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.