Evidence map›Paper›PMID 7616958›Full record

ArticleMolecular & general genetics : MGG1995

Sequencing and analysis of the gene encoding the alpha-toxin of Clostridium novyi proves its homology to toxins A and B of Clostridium difficile.

F Hofmann, A Herrmann, E Habermann, C von Eichel-Streiber

Abstract read
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In one paragraph

Article in Molecular & general genetics : MGG, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

11 citing papers in PubMed, 40 citations in OpenAlex.

  1. In silico vaccine design: Targeting highly epitopic regions ofComputational and structural biotechnology journal · 2024
    Article
  2. Article
  3. Large Clostridial Toxins: Mechanisms and Roles in Disease.Microbiology and molecular biology reviews : MMBR · 2021
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Translocation of Clostridium difficile toxin B across polarized Caco-2 cell monolayers is enhanced by toxin A.The Canadian journal of infectious diseases = Journal canadien des maladies infectieuses · 2004
    Article
  10. Combination bacteriolytic therapy for the treatment of experimental tumors.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  11. 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

4 authors at 2 institutions in 1 country.

F HofmannInstitut für Medizinische Mikrobiologie, Johannes Gutenberg-Universität Mainz, Germany.
A Herrmann
E Habermann
C von Eichel-Streiber
Johannes Gutenberg University Mainz · DEUniversity of Giessen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A library of total Clostridium novyi DNA was established and screened for the alpha-toxin gene (tcn alpha) by hybridization with oligonucleotides derived from a partial N-terminal sequence and by using specific antisera. Overlapping subgenic tcn alpha fragments were isolated and subsequently the total sequence of tcn alpha was determined. The 6534 nucleotide open reading frame encodes a polypeptide of M(r) 250,166 and pI 5.9. The N-terminal alpha-toxin (Tcn alpha) sequence MLITREQLMKIASIP determined by Edman degradation confirmed the identity of the reading frame and the assignment of the translation start point. The toxin is not modified posttranslationally at its N-terminus nor does it consist of different subunits. Overall the amino acid sequence shows 48% homology between the Tcn alpha and both toxins A (TcdA) and B (TcdB) of Clostridium difficile. The C-terminal 382 residues of Tcn alpha constitute a repetitive domain similar to those reported for TcdA and TcdB of C. difficile. The individual repeat motifs of these three toxins consist of oligopeptides some 19-52 amino acids in length, arranged in four to five different groups. Genetic, biochemical and pharmacological data thus confirm that the three toxins belong to one subgroup, designated large clostridial cytotoxins (LCT). Further definition of their structure and detailed molecular action should allow the LCTs to be used tools for the analysis of microfilament assembly and function.

Indexed as

Bacterial ProteinsAmino Acid SequenceBacterial ToxinsBase SequenceClostridioides difficileClostridiumEnterotoxinsGenomic LibraryMolecular Sequence DataRecombinant ProteinsSequence Homology, Amino AcidType C PhospholipasesBacterial ProteinsBacterial ToxinsEnterotoxinsRecombinant ProteinstcdA protein, Clostridium difficiletoxB protein, Clostridium difficileType C Phospholipases

Identifiers

PMID7616958
OpenAlexW1965980594

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.