Evidence map›Paper›PMID 26239840›Full record

ArticleBMC biotechnology2015

Production of recombinant VP1-derived virus-like particles from novel human polyomaviruses in yeast.

Milda Norkiene, Jomante Stonyte, Danguole Ziogiene, Egle Mazeike, Kestutis Sasnauskas, Alma Gedvilaite

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2015. 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
1.7field-weighted citation impact, top 14% 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, 30 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Highly stableFrontiers in bioengineering and biotechnology · 2024
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  12. Article
  13. Merkel cell polyomavirus and Merkel cell carcinoma.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  14. Review
  15. Article
  16. 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

6 authors at 1 institution in 1 country.

Milda NorkieneInstitute of Biotechnology, Vilnius University, Graiciuno 8, LT-02241, Vilnius, Lithuania. milda.norkiene@bti.vu.lt.
Jomante StonyteInstitute of Biotechnology, Vilnius University, Graiciuno 8, LT-02241, Vilnius, Lithuania. jomante@gmail.com.
Danguole ZiogieneInstitute of Biotechnology, Vilnius University, Graiciuno 8, LT-02241, Vilnius, Lithuania. danguole.ziogiene@bti.vu.lt.
Egle MazeikeInstitute of Biotechnology, Vilnius University, Graiciuno 8, LT-02241, Vilnius, Lithuania. egluzes@gmail.com.
Kestutis SasnauskasInstitute of Biotechnology, Vilnius University, Graiciuno 8, LT-02241, Vilnius, Lithuania. kestutis.sasnauskas@bti.vu.lt.
Alma GedvilaiteInstitute of Biotechnology, Vilnius University, Graiciuno 8, LT-02241, Vilnius, Lithuania. agedv@ibt.lt.
Vilnius University · LT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundEleven new human polyomaviruses (HPyVs) have been identified in the last decade. Serological studies show that these novel HPyVs sub-clinically infect humans at an early age. The routes of infection, entry pathways, and cell tropism of new HPyVs remain unknown. VP1 proteins of polyomaviruses can assembly into virus-like particles (VLPs). As cell culturing systems for HPyV are currently not available, VP1-derived VLPs may be useful tools in basic research and biotechnological applications.

resultsRecombinant VP1-derived VLPs from 11 newly identified HPyVs were efficiently expressed in yeast. VP1 proteins derived from Merkel cell polyomavirus (MCPyV), trichodysplasia spinulosa-associated polyomavirus (TSPyV), and New Jersey polyomavirus (NJPyV) self-assembled into homogeneous similarly-sized VLPs. Karolinska Institutet polyomavirus (KIPyV), HPyV7, HPyV9, HPyV10, and St. Louis polyomavirus (STLPyV) VP1 proteins formed VLPs that varied in size with diameters ranging from 20 to 60 nm. Smaller-sized VLPs (25-35 nm in diameter) predominated in preparations from Washington University polyomavirus (WUPyV) and HPyV6. Attempts to express recombinant HPyV12 VP1-derived VLPs in yeast indicate that translation of VP1 might start at the second of two potential translation initiation sites in the VP1-encoding open reading frame (ORF). This translation resulted in a 364-amino acid-long VP1 protein, which efficiently self-assembled into typical PyV VLPs. MCPyV-, KIPyV-, TSPyV-, HPyV9-, HPyV10-, and HPyV12-derived VLPs showed hemagglutination (HA) assay activity in guinea pig erythrocytes, whereas WUPyV-, HPyV6-, HPyV7-, STLPyV- and NJPyV-derived VP1 VLPs did not.

conclusionsThe yeast expression system was successfully utilized for high-throughput production of recombinant VP1-derived VLPs from 11 newly identified HPyVs. HPyV12 VP1-derived VLPs were generated from the second of two potential translation initiation sites in the VP1-encoding ORF. Recombinant VLPs produced in yeast originated from different HPyVs demonstrated distinct HA activities and may be useful in virus diagnostics, capsid structure studies, or investigation of entry pathways and cell tropism of HPyVs until cell culture systems for new HPyVs are developed.

Indexed as

Capsid ProteinsHumansPolyomavirusPolyomavirus InfectionsVirionCapsid Proteins

Identifiers

PMID26239840
PMCPMC4523907
OpenAlexW1768939513

What OpenQuestion holds

Textmetadata
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.