Evidence map›Paper›PMID 16775318›Full record

ArticleJournal of virology2006

The signal peptide of the ebolavirus glycoprotein influences interaction with the cellular lectins DC-SIGN and DC-SIGNR.

Andrea Marzi, Armin Akhavan, Graham Simmons, Thomas Gramberg, Heike Hofmann, Paul Bates, Vishwanath R Lingappa, Stefan Pöhlmann

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

40 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. The balance between gasdermin D and STING signaling shapes the severity of schistosome immunopathology.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  15. Article
  16. Analysis of Ebola Virus Entry Into Macrophages.The Journal of infectious diseases · 2015
    Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 4 institutions in 2 countries.

Andrea MarziInstitute for Clinical and Molecular Virology and Nikolaus-Fiebiger-Center, University Erlangen-Nürnberg, Glückstrasse 6, 91054 Erlangen, Germany.
Armin Akhavan
Graham Simmons
Thomas Gramberg
Heike Hofmann
Paul Bates
Vishwanath R Lingappa
Stefan Pöhlmann
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversity of Pennsylvania · USBlood Systems Research Institute · USCalifornia Pacific Medical Center · US

Funding

Vaccine strategy for broad spectrum protection agains non-typhoidal salmonellU54AI057168 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI WHITE, JUDITH M. · 2003 to 2013
$91.5M
NIAID NIH HHS U54 AI 057168NIAID NIH HHS U54 AI057168
6 · The paper itself

Abstract

The C-type lectins DC-SIGN and DC-SIGNR (collectively referred to as DC-SIGN/R) bind to the ebolavirus glycoprotein (EBOV-GP) and augment viral infectivity. DC-SIGN/R strongly enhance infection driven by the GP of EBOV subspecies. Zaire (ZEBOV) but have a much less pronounced effect on infection mediated by the GP of EBOV subspecies. Sudan (SEBOV). For this study, we analyzed the determinants of the differential DC-SIGN/R interactions with ZEBOV- and SEBOV-GP. The efficiency of DC-SIGN engagement by ZEBOV-GP was dependent on the rate of GP incorporation into lentiviral particles, while appreciable virion incorporation of SEBOV-GP did not allow robust DC-SIGN/R usage. Forced incorporation of high-mannose carbohydrates into SEBOV-GP augmented the engagement of DC-SIGN/R to the levels observed with ZEBOV-GP, indicating that appropriate glycosylation of SEBOV-GP is sufficient for efficient DC-SIGN/R usage. However, neither signals for N-linked glycosylation unique to SEBOV- or ZEBOV-GP nor the highly variable and heavily glycosylated mucin-like domain modulated the interaction with DC-SIGN/R. In contrast, analysis of chimeric GPs identified the signal peptide as a determinant of DC-SIGN/R engagement. Thus, ZEBOV- but not SEBOV-GP was shown to harbor high-mannose carbohydrates, and GP modification with these glycans was controlled by the signal peptide. These results suggest that the signal peptide governs EBOV-GP interactions with DC-SIGN/R by modulating the incorporation of high-mannose carbohydrates into EBOV-GP. In summary, we identified the level of GP incorporation into virions and signal peptide-controlled glycosylation of GP as determinants of attachment factor engagement.

Indexed as

Cell Adhesion MoleculesCell LineDC-Specific ICAM-3 Grabbing NonintegrinEbolavirusGlycosylationHemorrhagic Fever, EbolaHumansLectins, C-TypeLentivirusMannoseMucinsMutant Chimeric ProteinsProtein BindingProtein Modification, TranslationalProtein Sorting SignalsProtein Structure, TertiaryCell Adhesion MoleculesCLEC4M protein, humanDC-Specific ICAM-3 Grabbing Nonintegrinenvelope glycoprotein, Ebola virusLectins, C-TypeMannoseMucinsMutant Chimeric ProteinsProtein Sorting SignalsReceptors, Cell SurfaceViral Envelope Proteins

Identifiers

PMID16775318
PMCPMC1488929
OpenAlexW2152195875

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.