Evidence map›Paper›PMID 18824550›Full record

ArticleThe Journal of biological chemistry2008

Mycobacterium avium glycopeptidolipids require specific acetylation and methylation patterns for signaling through toll-like receptor 2.

Lindsay Sweet, Wenhui Zhang, Heidi Torres-Fewell, Anthony Serianni, William Boggess, Jeffrey Schorey

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
0.9field-weighted citation impact, top 27% 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, 31 citations in OpenAlex.

  1. Critical reviews in microbiology · 2026
    Review
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  4. Article
  5. Review
  6. Mutation onVirulence · 2020
    Article
  7. Article
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  9. Article
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  12. Innate defects of the IL-12/IFN-γ axis in susceptibility to infections by mycobacteria and salmonella.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2014
    Review
  13. Article
  14. Review
  15. Article
  16. Article
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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 1 country.

Lindsay SweetDepartment of Biological Sciences, Eck Center for Global Health and Infectious Disease, University of Notre Dame, Indiana 46556, USA.
Wenhui Zhang
Heidi Torres-Fewell
Anthony Serianni
William Boggess
Jeffrey Schorey
University of Notre Dame · USCenter for Global Health · US

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
M. avium GPLs in Macrophage Activation and VirulenceR01AI052439 · NIAID · UNIVERSITY OF NOTRE DAME · PI SCHOREY, JEFFREY SCOTT · 2004 to 2014
$3.4M
Macrophage signaling upon M avium infectionR01AI056979 · NIAID · UNIVERSITY OF NOTRE DAME · PI SCHOREY, JEFFREY SCOTT · 2004 to 2008
$1.4M
NIAID NIH HHS AI052439NIAID NIH HHS AI056979NIGMS NIH HHS T32GM075762
6 · The paper itself

Abstract

Toll-like receptors (TLRs) recognize pathogen-associated molecules and play a vital role in promoting an immune response against invading microbes. TLR2, one of the key members of the TLR family, recognizes a wide variety of microbial products, including lipoproteins and lipopeptides, from a number of pathogens. Recent studies from our laboratory indicate that glycopeptidolipids (GPLs), a major surface component of Mycobacterium avium and other non-tuberculosis mycobacteria, are ligands for TLR2. However, the molecular requirements necessary for the GPL-TLR2 interaction were not defined in this report. In the present study we isolated different GPL species from M. avium, and using mass spectrometry and NMR analyses, characterized the molecular requirements of the GPL-TLR2 interaction. Interestingly, the extent of the respective acetylation and methylation of the 6-deoxytalose and rhamnose contained within the core GPL structure dictated whether the GPL signaled through TLR2. These experiments illustrate how subtle changes in a complex TLR2 ligand can alter its affinity for this important receptor, and suggest that M. avium could potentially modify its GPL structure to limit its interaction with TLR2.

Indexed as

AcetylationAnimalsBacterial ProteinsCarbohydrate SequenceDeoxy SugarsGlycolipidsGlycoproteinsHexosesLigandsMacrophagesMethylationMiceMycobacterium aviumRhamnoseSignal TransductionStructure-Activity Relationship6-deoxytaloseBacterial ProteinsDeoxy SugarsGlycolipidsGlycoproteinsHexosesLigandsRhamnoseTlr2 protein, mouseToll-Like Receptor 2

Identifiers

PMID18824550
PMCPMC2586276
OpenAlexW1976120524

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.