Evidence map›Paper›PMID 16541102›Full record

ArticleThe EMBO journal2006

LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis.

Gerlind Sulzenbacher, Stéphane Canaan, Yann Bordat, Olivier Neyrolles, Gustavo Stadthagen, Véronique Roig-Zamboni, Jean Rauzier, Damien Maurin, Françoise Laval, Mamadou Daffé and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 134 citations in OpenAlex.

  1. Structure, assembly, and mechanism of the MmpL family of transporters.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Article
  3. Secreted proteins ofFrontiers in tuberculosis · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. The role of ABC transporter DrrABC in the export of PDIM inCell surface (Amsterdam, Netherlands) · 2024
    Article
  9. Article
  10. Article
  11. Microbiology spectrum · 2022
    Article
  12. Article
  13. Proteome characterization of the culture supernatant ofBiochemistry and biophysics reports · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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

14 authors at 5 institutions in 1 country.

Gerlind SulzenbacherAFMB, CNRS UMR 6098, Marseille Cedex, France.
Stéphane Canaan
Yann Bordat
Olivier Neyrolles
Gustavo Stadthagen
Véronique Roig-Zamboni
Jean Rauzier
Damien Maurin
Françoise Laval
Mamadou Daffé
Christian Cambillau
Brigitte Gicquel
Yves Bourne
Mary Jackson
Institut Pasteur · FRCentre National de la Recherche Scientifique · FRArchitecture et Fonction des Macromolécules Biologiques · 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

Cell envelope lipids play an important role in the pathogenicity of mycobacteria, but the mechanisms by which they are transported to the outer membrane of these prokaryotes are largely unknown. Here, we provide evidence that LppX is a lipoprotein required for the translocation of complex lipids, the phthiocerol dimycocerosates (DIM), to the outer membrane of Mycobacterium tuberculosis. Abolition of DIM transport following disruption of the lppX gene is accompanied by an important attenuation of the virulence of the tubercle bacillus. The crystal structure of LppX unveils an U-shaped beta-half-barrel dominated by a large hydrophobic cavity suitable to accommodate a single DIM molecule. LppX shares a similar fold with the periplasmic molecular chaperone LolA and the outer membrane lipoprotein LolB, which are involved in the localization of lipoproteins to the outer membrane of Gram-negative bacteria. Based on the structure and although an indirect participation of LppX in DIM transport cannot yet be ruled out, we propose LppX to be the first characterized member of a family of structurally related lipoproteins that carry lipophilic molecules across the mycobacterial cell envelope.

Indexed as

AnimalsBiological TransportCell MembraneCrystallography, X-RayFemaleHydrophobic and Hydrophilic InteractionsLipidsLipoproteinsLungMiceMice, Inbred BALB CModels, MolecularMutationMycobacterium tuberculosisProtein ConformationProtein FoldingLipidsLipoproteinsphthiocerol dimycocerosate

Identifiers

PMID16541102
PMCPMC1440309
OpenAlexW2119069290

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.