Evidence map›Paper›PMID 15304515›Full record

ArticleThe Journal of biological chemistry2004

A novel sorting signal for intracellular localization is present in the S protein of a porcine coronavirus but absent from severe acute respiratory syndrome-associated coronavirus.

Christel Schwegmann-Wessels, Marwan Al-Falah, David Escors, Zai Wang, Gert Zimmer, Hongkui Deng, Luis Enjuanes, Hassan Y Naim, Georg Herrler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 58 citations in OpenAlex.

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  9. The molecular virology of coronaviruses.The Journal of biological chemistry · 2020
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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

9 authors at 4 institutions in 4 countries.

Christel Schwegmann-WesselsInstitut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, D-30559, Germany.
Marwan Al-Falah
David Escors
Zai Wang
Gert Zimmer
Hongkui Deng
Luis Enjuanes
Hassan Y Naim
Georg Herrler
Consejo Superior de Investigaciones Científicas · ESInstitut de Virologie · FRPeking University · CNUniversity of Veterinary Medicine Hannover, Foundation · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coronaviruses (CoV) mature by a budding process at intracellular membranes. Here we showed that the major surface protein S of a porcine CoV (transmissible gastroenteritis virus) is not transported to the cell surface but is retained intracellularly. Site-directed mutagenesis indicated that a tyrosine-dependent signal (YXXI) in the cytoplasmic tail is essential for intracellular localization of the S protein. Surface expression of mutant proteins was evident by immunofluorescence analysis and surface biotinylation. Intracellularly retained S proteins only contained endoglycosidase H-sensitive N-glycans, whereas mutant proteins that migrated to the plasma membrane acquired N-linked oligosaccharides of the complex type. Corresponding tyrosine residues are present in the cytoplasmic tails of the S proteins of other animal CoV but not in the tail portion of the S protein of severe acute respiratory syndrome (SARS)-CoV. Changing the SEPV tetrapeptide in the cytoplasmic tail to YEPI resulted in intracellular retention of the S protein of SARS-CoV. As the S proteins of CoV have receptor binding and fusion activities and are the main target of neutralizing antibodies, the differences in the transport behavior of the S proteins suggest different strategies in the virus host interactions between SARS-CoV and other coronaviruses.

Indexed as

Amino Acid SubstitutionAnimalsBase SequenceCoronavirusDNA PrimersMembrane GlycoproteinsMolecular Sequence DataMutagenesis, Site-DirectedRespiratory Distress SyndromeSpike Glycoprotein, CoronavirusSwineViral Envelope ProteinsDNA PrimersMembrane GlycoproteinsSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, mouse hepatitis virusViral Envelope Proteins

Identifiers

PMID15304515
PMCPMC8060824
OpenAlexW2009349433

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.