Evidence map›Paper›PMID 16737539›Full record

ArticleVirology journal2006

The role of single N-glycans in proteolytic processing and cell surface transport of the Lassa virus glycoprotein GP-C.

Robert Eichler, Oliver Lenz, Wolfgang Garten, Thomas Strecker

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

47 citing papers in PubMed, 73 citations in OpenAlex.

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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

4 authors at 1 institution in 2 countries.

Robert EichlerInstitut für Virologie der Philipps-Universität Marburg, Hans-Meerwein-Str, 3, 35037 Marburg, Germany. Robert.Eichler@abbott.com
Oliver Lenz
Wolfgang Garten
Thomas Strecker
Philipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lassa virus glycoprotein is synthesised as a precursor (preGP-C) into the lumen of the endoplasmic reticulum. After cotranslational cleavage of the signal peptide, the immature GP-C is posttranslationally processed into the N-terminal subunit GP-1 and the C-terminal subunit GP-2 by the host cell subtilase SKI-1/S1P. The glycoprotein precursor contains eleven potential N-glycosylation sites. In this report, we investigated the effect of each N-glycan on proteolytic cleavage and cell surface transport by disrupting the consensus sequences of eleven potential N-glycan attachment sites individually. Five glycoprotein mutants with disrupted N-glycosylation sites were still proteolytically processed, whereas the remaining N-glycosylation sites are necessary for GP-C cleavage. Despite the lack of proteolytic processing, all cleavage-defective mutants were transported to the cell surface and remained completely endo H-sensitive. The findings indicate that N-glycans are needed for correct conformation of GP-C in order to be cleaved by SKI-1/S1P.

Indexed as

AnimalsCell MembraneChlorocebus aethiopsGlycoproteinsGlycosylationLassa virusMutationPolysaccharidesProprotein ConvertasesProtein ConformationProtein FoldingProtein PrecursorsSerine EndopeptidasesTransfectionVero CellsViral Envelope Proteinsglycoprotein gp1, lassa virusglycoprotein gp2, lassa virusGlycoproteinsmembrane-bound transcription factor peptidase, site 1PolysaccharidesProprotein ConvertasesProtein PrecursorsSerine EndopeptidasesViral Envelope Proteins

Identifiers

PMID16737539
PMCPMC1524727
OpenAlexW2161122489

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.