Evidence map›Paper›PMID 18390543›Full record

ArticleThe Journal of biological chemistry2008

Deciphering the genetic bases of the structural diversity of phenolic glycolipids in strains of the Mycobacterium tuberculosis complex.

Wladimir Malaga, Patricia Constant, Daniel Euphrasie, Angel Cataldi, Mamadou Daffé, Jean-Marc Reyrat, Christophe Guilhot

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Anti-phenolic glycolipid antibodies inOne health (Amsterdam, Netherlands) · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. The cell envelope glycoconjugates of Mycobacterium tuberculosis.Critical reviews in biochemistry and molecular biology
    Review
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

7 authors at 5 institutions in 1 country.

Wladimir MalagaUniversité Paul Sabatier and CNRS, Institut de Pharmacologie et Biologie Structurale (Unité Mixte de Recherche 5089), Département Mécanismes Moléculaires des Infections Mycobactériennes, 205 Route de Narbonne, Toulouse Cedex 4, France.
Patricia Constant
Daniel Euphrasie
Angel Cataldi
Mamadou Daffé
Jean-Marc Reyrat
Christophe Guilhot
Délégation Paris 5 · FRInserm · FRInstitut d'Économie Industrielle · FRInstitut de Pharmacologie et de Biologie Structurale · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phenolic glycolipids (PGL) play a major role in the virulence of mycobacteria, notably in strains of the Mycobacterium tuberculosis complex and in Mycobacterium leprae. The structure of the carbohydrate domain of these compounds is highly variable, and the genetic bases for these variations remain unknown. We demonstrated that the monoglycosylated PGL formed by Mycobacterium bovis differs from the triglycosylated PGL synthesized by M. tuberculosis (PGL-tb) because of the following two genetic defects: a frameshift mutation within the gene Rv2958c, encoding a glycosyltransferase involved in the transfer of the second rhamnosyl residue of the PGL-tb, and a deletion of a region that encompasses two genes, which encode a GDP-D-mannose 4,6-dehydratase and a GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase/reductase, required for the formation of activated L-fucose. Expression of these three genes in M. bovis BCG allowed synthesis of PGL-tb in this recombinant strain. Additionally, we showed that all M. bovis, Mycobacterium microti, Mycobacterium pinnipedii, and some Mycobacterium africanum strains harbor the same frameshift mutation in their Rv2958c orthologs. Consistently, the structure of PGLs purified from M. africanum (harboring the Rv2958c mutation) and M. pinnipedii strains revealed that these compounds are monoglycosylated PGL. These findings explain the specificity of PGL-tb production by some strains of the M. tuberculosis complex and have important implications for our understanding of the evolution of this complex.

Indexed as

Evolution, MolecularAntigens, BacterialCarbohydrate EpimerasesFrameshift MutationFucoseGlycolipidsGlycosyltransferasesHydro-LyasesMycobacterium bovisMycobacterium lepraeMycobacterium tuberculosisSpecies SpecificityVirulence FactorsAntigens, BacterialCarbohydrate EpimerasesFucoseGDPmannose 4,6-dehydrataseGlycolipidsGlycosyltransferasesHydro-Lyasesphenolic glycolipid I, Mycobacterium lepraeRv2958c protein, Mycobacterium tuberculosisVirulence Factors

Identifiers

PMID18390543
PMCPMC3258887
OpenAlexW1975551443

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.