Evidence map›Paper›PMID 33731457›Full record

ArticleJournal of virology2021

Human Papillomavirus infection requires the CCT Chaperonin Complex.

Marina Bugnon Valdano, Paola Massimi, Justyna Broniarczyk, David Pim, Michael Myers, Daniela Gardiol, Lawrence Banks

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 19 citations in OpenAlex.

  1. Chaperonin in health and disease.Molecular biomedicine · 2026
    Review
  2. Article
  3. bioRxiv : the preprint server for biology · 2025
    Article
  4. Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022
    Review
  14. Review
  15. Review
  16. Review
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 2 institutions in 3 countries.

Marina Bugnon ValdanoTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Paola MassimiTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Justyna BroniarczykTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
David PimTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Michael MyersProtein Networks, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Daniela GardiolInstituto de Biología Molecular y Celular de Rosario-CONICET, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
Lawrence BanksTumour Virology Laboratory, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy banks@icgeb.org.
International Centre for Genetic Engineering and Biotechnology · ITNational University of Rosario · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human papillomavirus (HPV) infection is a multi-step process that implies complex interactions of the viral particles with cellular proteins. The HPV capsid includes the two structural proteins L1 and L2, that play crucial roles on infectious viral entry. L2 is particularly relevant for the intracellular trafficking of the viral DNA towards the nucleus. Here, using proteomic studies we identified CCT proteins as novel interaction partners of HPV-16 L2. The CCT multimeric complex is an essential chaperonin which interacts with a large number of protein targets. We analysed the binding of different components of the CCT complex to L2. We confirmed the interaction of this structural viral protein with the CCT subunit 3 (CCT3) and we found that this interaction requires the N-terminal region of L2. Defects in HPV-16 pseudoviral particle (PsVs) infection were revealed by siRNA-mediated knockdown of some CCT subunits. While a substantial drop in the viral infection was associated with the ablation of CCT component 2, even more pronounced effects on infectivity were observed upon depletion of CCT component 3. Using confocal immunofluorescence assays, CCT3 co-localised with HPV PsVs at early times after infection, with L2 being required for this to occur. Further analysis showed the colocalization of several other subunits of CCT with the PsVs. Moreover, we observed a defect in capsid uncoating and a change in PsVs intracellular normal processing when ablating CCT3. Taken together, these studies demonstrate the importance of CCT chaperonin during HPV infectious entry.

Identifiers

PMID33731457
PMCPMC8139704
OpenAlexW3137797923

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.