Evidence map›Paper›PMID 22045808›Full record

ArticleThe Journal of biological chemistry2011

Mimivirus collagen is modified by bifunctional lysyl hydroxylase and glycosyltransferase enzyme.

Kelvin B Luther, Andreas J Hülsmeier, Belinda Schegg, Stefan A Deuber, Didier Raoult, Thierry Hennet

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Crystal Structure ofBiochemistry · 2025
    Article
  6. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  7. Structure of an FeActa crystallographica. Section F, Structural biology communications · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022
    Review
  16. Article
  17. Exploitation of glycosylation in enveloped virus pathobiology.Biochimica et biophysica acta. General subjects · 2019
    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

6 authors at 2 institutions in 2 countries.

Kelvin B LutherInstitute of Physiology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Andreas J HülsmeierInstitute of Physiology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Belinda ScheggInstitute of Physiology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Stefan A DeuberInstitute of Physiology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Didier RaoultUnité de Recherche sur les Maladies Infectieuses et Tropicales Émergentes, CNRS Unité Mixte de Recherche Institut de Recherche pour le Développement 6236, Faculté de Médecine, Université de la Méditerranée, 13385 Marseille cedex 5, France.
Thierry HennetInstitute of Physiology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland. Electronic address: thennet@access.uzh.ch.
University of Zurich · CHCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagens, the most abundant proteins in animals, are modified by hydroxylation of proline and lysine residues and by glycosylation of hydroxylysine. Dedicated prolyl hydroxylase, lysyl hydroxylase, and collagen glycosyltransferase enzymes localized in the endoplasmic reticulum mediate these modifications prior to the formation of the collagen triple helix. Whereas collagen-like proteins have been described in some fungi, bacteria, and viruses, the post-translational machinery modifying collagens has never been described outside of animals. We demonstrate that the L230 open reading frame of the giant virus Acanthamoeba polyphaga mimivirus encodes an enzyme that has distinct lysyl hydroxylase and collagen glycosyltransferase domains. We show that mimivirus L230 is capable of hydroxylating lysine and glycosylating the resulting hydroxylysine residues in a native mimivirus collagen acceptor substrate. Whereas in animals from sponges to humans the transfer of galactose to hydroxylysine in collagen is conserved, the mimivirus L230 enzyme transfers glucose to hydroxylysine, thereby defining a novel type of collagen glycosylation in nature. The presence of hydroxylysine in mimivirus proteins was confirmed by amino acid analysis of mimivirus recovered from A. polyphaga cultures. This work shows for the first time that collagen post-translational modifications are not confined to the domains of life. The utilization of glucose instead of the galactose found throughout animals as well as a bifunctional enzyme rather than two separate enzymes may represent a parallel evolutionary track in collagen biology. These results suggest that giant viruses may have contributed to the evolution of collagen biology.

Indexed as

AcanthamoebaAmino Acid SequenceAnimalsBaculoviridaeCloning, MolecularCollagenGenetic VectorsGlycosylationGlycosyltransferasesHumansHydroxylysineMimiviridaeMolecular Sequence DataOpen Reading FramesProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseProtein Processing, Post-TranslationalCollagenGlycosyltransferasesHydroxylysineProcollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase

Identifiers

PMID22045808
PMCPMC3243560
OpenAlexW2023047498

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.