Evidence map›Paper›PMID 21931730›Full record

ArticlePloS one2011

BKV agnoprotein interacts with α-soluble N-ethylmaleimide-sensitive fusion attachment protein, and negatively influences transport of VSVG-EGFP.

Mona Johannessen, Mari Walquist, Nancy Gerits, Marte Dragset, Anne Spang, Ugo Moens

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. BK polyomavirus: latency, reactivation, diseases and tumorigenesis.Frontiers in cellular and infection microbiology · 2023
    Review
  4. Review
  5. Review
  6. Human polyomaviruses and cancer: an overview.Clinics (Sao Paulo, Brazil) · 2018
    Review
  7. Agnoprotein Is an Essential Egress Factor during BK Polyomavirus Infection.International journal of molecular sciences · 2018
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

6 authors at 2 institutions in 2 countries.

Mona JohannessenResearch Group of Host-Microbe Interactions, Department of Medical Biology, Faculty of Health Sciences, University of Tromsø, Tromsø, Norway. mona.johannessen@uit.no
Mari Walquist
Nancy Gerits
Marte Dragset
Anne Spang
Ugo Moens
UiT The Arctic University of Norway · NOUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe human polyomavirus BK (BKV) infects humans worldwide and establishes a persistent infection in the kidney. The BK virus genome encodes three regulatory proteins, large and small tumor-antigen and the agnoprotein, as well as the capsid proteins VP1 to VP3. Agnoprotein is conserved among BKV, JC virus (JCV) and SV40, and agnoprotein-deficient mutants reveal reduced viral propagation. Studies with JCV and SV40 indicate that their agnoproteins may be involved in transcription, replication and/or nuclear and cellular release of the virus. However, the exact function(s) of agnoprotein of BK virus remains elusive. PRINCIPAL

findingsAs a strategy of exploring the functions of BKV agnoprotein, we decided to look for cellular interaction partners for the viral protein. Several partners were identified by yeast two-hybrid assay, among them α-SNAP which is involved in disassembly of vesicles during secretion. BKV agnoprotein and α-SNAP were found to partially co-localize in cells, and a complex consisting of agnoprotein and α-SNAP could be co-immunoprecipitated from cells ectopically expressing the proteins as well as from BKV-transfected cells. The N-terminal part of the agnoprotein was sufficient for the interaction with α-SNAP. Finally, we could show that BKV agnoprotein negatively interferes with secretion of VSVG-EGFP reporter suggesting that agnoprotein may modulate exocytosis.

conclusionsWe have identified the first cellular interaction partner for BKV agnoprotein. The most N-terminal part of BKV agnoprotein is involved in the interaction with α-SNAP. Presence of BKV agnoprotein negatively interferes with secretion of VSVG-EGFP reporter.

Indexed as

Antigens, NeoplasmBK VirusExocytosisGenome, ViralGreen Fluorescent ProteinsHEK293 CellsHumansKidneyMembrane GlycoproteinsMicroscopy, FluorescencePlasmidsProtein Structure, TertiarySoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsTwo-Hybrid System TechniquesViral Envelope ProteinsViral Proteinsagnoprotein, polyomavirusAntigens, Neoplasmenhanced green fluorescent proteinG protein, vesicular stomatitis virusGreen Fluorescent ProteinsMembrane GlycoproteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsViral Envelope ProteinsViral ProteinsViral Regulatory and Accessory ProteinsViroporin Proteins

Identifiers

PMID21931730
PMCPMC3171462
OpenAlexW1993538815

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.