Evidence map›Paper›PMID 22435790›Full record

ArticleMolecular microbiology2012

Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid.

Lina Kandiba, Olli Aitio, Jari Helin, Ziqiang Guan, Perttu Permi, Dennis H Bamford, Jerry Eichler, Elina Roine

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

28 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Glycoproteins in Viruses.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  3. Journal of bacteriology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Viruses · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018
    Article
  14. Article
  15. Article
  16. Exploration of the Sialic Acid World.Advances in carbohydrate chemistry and biochemistry · 2018
    Review
  17. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  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 3 countries.

Lina KandibaDepartment of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.
Olli Aitio
Jari Helin
Ziqiang Guan
Perttu Permi
Dennis H Bamford
Jerry Eichler
Elina Roine
University of Helsinki · FIBen-Gurion University of the Negev · ILDuke University Hospital · USGlykos (Finland) · FI

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
NIGMS NIH HHS GM-069338NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

VP4, the major structural protein of the haloarchaeal pleomorphic virus, HRPV-1, is glycosylated. To define the glycan structure attached to this protein, oligosaccharides released by β-elimination were analysed by mass spectrometry and nuclear magnetic resonance spectroscopy. Such analyses showed that the major VP4-derived glycan is a pentasaccharide comprising glucose, glucuronic acid, mannose, sulphated glucuronic acid and a terminal 5-N-formyl-legionaminic acid residue. This is the first observation of legionaminic acid, a sialic acid-like sugar, in an archaeal-derived glycan structure. The importance of this residue for viral infection was demonstrated upon incubation with N-acetylneuraminic acid, a similar monosaccharide. Such treatment reduced progeny virus production by half 4 h post infection. LC-ESI/MS analysis confirmed the presence of pentasaccharide precursors on two different VP4-derived peptides bearing the N-glycosylation signal, NTT. The same sites modified by the native host, Halorubrum sp. strain PV6, were also recognized by the Haloferax volcanii N-glycosylation apparatus, as determined by LC-ESI/MS of heterologously expressed VP4. Here, however, the N-linked pentasaccharide was the same as shown to decorate the S-layer glycoprotein in this species. Hence, N-glycosylation of the haloarchaeal viral protein, VP4, is host-specific. These results thus present additional examples of archaeal N-glycosylation diversity and show the ability of Archaea to modify heterologously expressed proteins.

Indexed as

Amino Acid SequenceArchaeal VirusesGlycosylationHaloferax volcaniiMass SpectrometryMolecular Sequence DataPeptide MappingPolysaccharidesSialic AcidsViral Proteins5,7-diacetamido-8-O-acetyl-3,5,7,9-tetradeoxy-glycero-talo-nonulosonic acidPolysaccharidesSialic AcidsViral Proteins

Identifiers

PMID22435790
PMCPMC3422550
OpenAlexW2124198448

What OpenQuestion holds

Textmetadata
LicenceTDM
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.