Evidence map›Paper›PMID 11705966›Full record

ArticleInfection and immunity2001

Localization of functional domains of the mitogenic toxin of Pasteurella multocida.

G D Pullinger, R Sowdhamini, A J Lax

Abstract readComparative Study
In one paragraph

Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  5. Review
  6. Substrate specificity of Pasteurella multocida toxin for α subunits of heterotrimeric G proteins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
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  13. Review
  14. Article
  15. Expression of 4 truncated fragments of Pasteurella multocida toxin and their immunogenicity.Canadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2009
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

3 authors at 3 institutions in 2 countries.

G D PullingerDepartment of Oral Microbiology, Kings College London, Guy's Hospital, London SE1 9RT, United Kingdom. gillian.pullinger@kcl.ac.uk
R Sowdhamini
A J Lax
Guy's Hospital · GBKing's College - North Carolina · USUniversity of Cambridge · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The locations of the catalytic and receptor-binding domains of the Pasteurella multocida toxin (PMT) were investigated. N- and C-terminal fragments of PMT were cloned and expressed as fusion proteins with affinity tags. Purified fusion proteins were assessed in suitable assays for catalytic activity and cell-binding ability. A C-terminal fragment (amino acids 681 to 1285) was catalytically active. When microinjected into quiescent Swiss 3T3 cells, it induced changes in cell morphology typical of toxin-treated cells and stimulated DNA synthesis. An N-terminal fragment with a His tag at the C terminus (amino acids 1 to 506) competed with full-length toxin for binding to surface receptors and therefore contains the cell-binding domain. The inactive mutant containing a mutation near the C terminus (C1165S) also bound to cells in this assay. Polyclonal antibodies raised to the N-terminal PMT region bound efficiently to full-length native toxin, suggesting that the N terminus is surface located. Antibodies to the C terminus of PMT were microinjected into cells and inhibited the activity of toxin added subsequently to the medium, confirming that the C terminus contains the active site. Analysis of the PMT sequence predicted a putative transmembrane domain with predicted hydrophobic and amphipathic helices near the N terminus over the region of homology to the cytotoxic necrotizing factors. The C-terminal end of PMT was predicted to be a mixed alpha/beta domain, a structure commonly found in catalytic domains. Homology to proteins of known structure and threading calculations supported these assignments.

Indexed as

Bacterial ProteinsTransglutaminasesVirulence Factors, Bordetella3T3 CellsAnimalsBacterial ToxinsCatalytic DomainCytotoxinsMiceMitogensPasteurella multocidaPeptide FragmentsProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Cell SurfaceBacterial ProteinsBacterial ToxinsCytotoxinsdermonecrotic toxin, BordetellaMitogensPasteurella multocida toxinPeptide FragmentsReceptors, Cell SurfaceRecombinant Fusion ProteinsTransglutaminasesVirulence Factors, Bordetella

Identifiers

PMID11705966
PMCPMC98880
OpenAlexW2136107008

What OpenQuestion holds

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Registered trials

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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.