Evidence map›Paper›PMID 7637027›Full record

ArticleJournal of virology1995

Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form.

S L Allison, K Stadler, C W Mandl, C Kunz, F X Heinz

Abstract read
In one paragraph

Article in Journal of virology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing 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

104 citing papers in PubMed.

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44 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.

S L AllisonInstitute of Virology, University of Vienna, Austria.
K Stadler
C W Mandl
C Kunz
F X Heinz

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A quantitative study was performed to investigate the requirements for secretion of recombinant soluble and particulate forms of the envelope glycoprotein E of tick-borne encephalitis (TBE) virus. Full-length E and a carboxy terminally truncated anchor-free form were expressed in COS cells in the presence and absence of prM, the precursor of the viral membrane protein M. Formation of a heteromeric complex with prM was found to be necessary for efficient secretion of both forms of E, whereas only low levels of anchor-free E were secreted in the absence of prM. The prM-mediated transport function could also be provided by coexpression of prM and E from separate constructs, but a prM-to-E ratio of greater than 1:1 did not further enhance secretion. Full-length E formed stable intracellular heterodimers with prM and was secreted as a subviral particle, whereas anchor-free E was not associated with particles and formed a less stable complex with prM, suggesting that prM interacts with both the ectodomain and anchor region of E.

Indexed as

AnimalsAntibodies, MonoclonalCell LineChlorocebus aethiopsElectrophoresis, Polyacrylamide GelEncephalitis Virus, Eastern EquineFlavivirusGene ExpressionImmunoblottingKidneyKineticsMacromolecular SubstancesMolecular WeightRecombinant ProteinsTransfectionViral Envelope ProteinsAntibodies, Monoclonalglycoprotein E, FlavivirusMacromolecular SubstancesRecombinant ProteinsViral Envelope Proteins

Identifiers

PMID7637027
PMCPMC189449

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.