Evidence map›Paper›PMID 2105289›Full record

ArticleJournal of bacteriology1990

Peptidoglycan-associated polypeptides of Mycobacterium tuberculosis.

G R Hirschfield, M McNeil, P J Brennan

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.7field-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

52 citing papers in PubMed, 123 citations in OpenAlex.

  1. The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Antigen specificity shapes antibody functions in tuberculosis.bioRxiv : the preprint server for biology · 2024
    Article
  5. International journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Extraction and Separation of Mycobacterial Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. 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

3 authors at 1 institution in 1 country.

G R HirschfieldDepartment of Microbiology, Colorado State University, Fort Collins 80523.
M McNeil
P J Brennan
Colorado State University · US

Funding

SURFACE ANTIGENS OF M LEPRAE AND OTHER MYCOBACTERIAR37AI018357 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BRENNAN, PATRICK JOSEPH · 1988 to 2007
$2.7M
MYOCOBACTERIAL CELL WALL AND DRUG DISCOVERYR01AI018357 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BRENNAN, PATRICK JOSEPH · 1998 to 2000
$421k
DEFINED NATIVE ANTIGENS AND IMMUNITY TO TUBERCULOSISR01AI027288 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BRENNAN, PATRICK JOSEPH · 1989 to 1993
–
SPECIFIC ANTIGENS OF ATYPICAL MYCOBACTERIAR22AI018357 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BRENNAN, PATRICK JOSEPH · 1985 to 1987
–
NIAID NIH HHS AI-18357NIAID NIH HHS AI-27288
6 · The paper itself

Abstract

Important protein-based immunoreactivities have long been associated with the cell wall core of mycobacteria. In order to explore the molecular basis of such activities, purified cell walls of Mycobacterium tuberculosis were extracted with sodium dodecyl sulfate to produce an insoluble residue composed of the mycolylarabinogalactan-peptidoglycan complex and about 2% of unextractable protein. Treatment of the product from an avirulent strain of M. tuberculosis with trifluoromethanesulfonic acid released a single polypeptide with a molecular size of 23 kilodaltons, accounting for all of the insoluble cell wall protein. Extensive purification and then analysis of the 23-kilodalton protein demonstrated the absence of diaminopimelic acid, muramic acid, or other peptidoglycan components, pointing to either a novel linkage between protein and peptidoglycan or a noncovalent but tenacious association. The released 23-kilodalton protein showed amino acid homology and other similarities to the outer membrane protein OmpF of Escherichia coli. Although a similar product was released in small quantities from cell walls of the virulent M. tuberculosis Erdman and H37Rv by lysozyme treatment, the cell walls of virulent bacilli were dominated by the presence of poly-alpha-L-glutamine, accounting for as much as 10% of their weight. The poly-alpha-L-glutamine was successfully separated from the cell wall proper, demonstrating again the absence of a covalent association between peptidoglycan and the polymer. The antigenicity of these products is demonstrated, and their roles vis-a-vis analogous polypeptides from other bacteria in immunogenicity, pathogenicity, and bacterial physiology are discussed.

Indexed as

Amino AcidsBlotting, WesternCell WallChromatography, GasChromatography, High Pressure LiquidEnzyme-Linked Immunosorbent AssayMicroscopy, ElectronMolecular WeightMycobacterium tuberculosisPeptidesPeptidoglycanTrypsinAmino AcidsPeptidesPeptidoglycanTrypsin

Identifiers

PMID2105289
PMCPMC208529
OpenAlexW1942250253

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.