Evidence map›Paper›PMID 18842962›Full record

ArticleGlycobiology2009

N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC.

Mark J Sartain, John T Belisle

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Establishment of minimum protein standards forMycobacteria (London, England) · 2025
    Article
  3. Article
  4. Article
  5. Evolution of Drug-ResistantFrontiers in microbiology · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Lipoprotein Glycosylation by Protein-Frontiers in microbiology · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  16. Article
  17. Review
  18. Article
  19. Bacterial protein-O-mannosylating enzyme is crucial for virulence of Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

2 authors at 1 institution in 1 country.

Mark J SartainDepartment of Microbiology, Immunology, and Pathology, Mycobacteria Research Laboratories, Colorado State University, Fort Collins, CO 80523, USA.
John T Belisle
Colorado State University · US

Funding

Antibody Based Diagnosis for TBR01AI056257 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI LAAL, SUMAN · 2003 to 2007
$2.0M
TUBERCULOSIS RESEARCH MATERIALS AND VACINE TESTINGN01AI075320 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · 1997 to 2004
$980k
NIAID NIH HHS N01 AI-75320NIAID NIH HHS R01 AI-056257PHS HHS HHSN26620040091C
6 · The paper itself

Abstract

SodC is one of two superoxide dismutases produced by Mycobacterium tuberculosis. This protein was previously shown to contribute to virulence and to act as a B-cell antigen. SodC is also a putative lipoprotein, and like other Sec-translocated mycobacterial proteins it was suggested to be modified with glycosyl units. To definitively define the glycosylation of SodC, we applied an approach that combined site-directed mutagenesis, lectin binding, and mass spectrometry. This resulted in identification of six O-glycosylated residues within a 13-amino-acid region near the N-terminus. Each residue was modified with one to three hexose units, and the most dominant SodC glycoform was modified with nine hexose units. In addition to O-glycosylation of threonine residues, this study provides the first evidence of serine O-glycosylation in mycobacteria. When combined with bioinformatic analyses, the clustering of O-glycosylation appeared to occur in a region of SodC with a disordered structure and not in regions important to the enzymatic activity of SodC. The use of recombinant amino acid substitutions to alter glycosylation sites provided further evidence that glycosylation influences proteolytic processing and ultimately positioning of cell wall proteins.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBacterial ProteinsGlycosylationLipoproteinsMass SpectrometryMolecular Sequence DataMycobacterium tuberculosisSuperoxide DismutaseBacterial ProteinsLipoproteinsSuperoxide Dismutase

Identifiers

PMID18842962
PMCPMC2733778
OpenAlexW2145438590

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.