Evidence map›Paper›PMID 19656298›Full record

ArticleMolecular microbiology2009

Genetic determination of essential residues of the Vibrio cholerae actin cross-linking domain reveals functional similarity with glutamine synthetases.

Brett Geissler, Amanda Bonebrake, Kerri-Lynn Sheahan, Margaret E Walker, Karla J F Satchell

Abstract read
In one paragraph

Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Antagonistic effects of actin-specific toxins onbioRxiv : the preprint server for biology · 2024
    Article
  3. Actin Cross-Linking Effector Domain of theInfection and immunity · 2022
    Article
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  5. Review
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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

5 authors at 4 institutions in 2 countries.

Brett GeisslerDepartment of Microbiology-Immunology, Northwestern University, Chicago, IL 60611, USA.
Amanda Bonebrake
Kerri-Lynn Sheahan
Margaret E Walker
Karla J F Satchell
Bipar · FRNorthwestern University · USTufts University · USUniversity of Chicago · US

Funding

TRAINING PROGRAM IN IMMUNOLOGY &MOLECULAR PATHOGENESIST32AI007476 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Edward Benjamin Thorp · 1996 to 2026
$6.6M
Genetic and biochemical study ov V. cholerase RTX toxinR01AI051490 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SATCHELL, KARLA J F · 2003 to 2012
$3.3M
NIAID NIH HHS AI051490NIAID NIH HHS R01 AI051490NIAID NIH HHS T32 AI007476NIAID NIH HHS T32-AI007476-11
6 · The paper itself

Abstract

Actin cross-linking domains (ACDs) are distinct domains found in several bacterial toxins, including the Vibrio cholerae MARTX toxin. The ACD of V. cholerae (ACD(Vc)) catalyses the formation of an irreversible iso-peptide bond between lysine 50 and glutamic acid 270 on two actin molecules in an ATP- and Mg/Mn(2+)-dependent manner. In vivo, cross-linking depletes the cellular pool of G-actin leading to actin cytoskeleton depolymerization. While the actin cross-linking reaction performed by these effector domains has been significantly characterized, the ACD(Vc) catalytic site has remained elusive due to lack of significant homology to known proteins. Using multiple genetic approaches, we have identified regions and amino acids of ACD(Vc) required for full actin cross-linking activity. Then, using these functional data and structural homology predictions, it was determined that several residues demonstrated to be important for ACD(Vc) activity are conserved with active-site residues of the glutamine synthetase family of enzymes. Thus, the ACDs are a family of bacterial toxin effectors that may be evolutionarily related to ligases involved in amino acid biosynthesis.

Indexed as

ActinsAmino Acid SequenceBacterial ToxinsCatalytic DomainConserved SequenceGlutamate-Ammonia LigaseModels, MolecularProtein Structure, TertiarySequence Homology, Amino AcidVibrio choleraeActinsBacterial ToxinsGlutamate-Ammonia Ligase

Identifiers

PMID19656298
PMCPMC2747471
OpenAlexW1976024911

What OpenQuestion holds

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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.