Evidence map›Paper›PMID 36038560›Full record

ArticleNature communications2022

Proteolytic processing induces a conformational switch required for antibacterial toxin delivery.

Nicholas L Bartelli, Victor J Passanisi, Karolina Michalska, Kiho Song, Dinh Q Nhan, Hongjun Zhou, Bonnie J Cuthbert, Lucy M Stols, William H Eschenfeldt, Nicholas G Wilson and 11 more

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
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  4. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

21 authors at 3 institutions in 1 country.

Nicholas L BartelliDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.ORCID http://orcid.org/0000-0001-6813-3684
Victor J PassanisiDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
Karolina MichalskaMidwest Center for Structural Genomics, Argonne National Laboratory, Lemont, IL, USA.ORCID http://orcid.org/0000-0001-7140-3649
Kiho SongBiomolecular Science and Engineering Program, University of California, Santa Barbara, CA, USA.
Dinh Q NhanDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, USA.
Hongjun ZhouDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
Bonnie J CuthbertDepartment of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.ORCID http://orcid.org/0000-0001-5176-8245
Lucy M StolsMidwest Center for Structural Genomics, Argonne National Laboratory, Lemont, IL, USA.
William H EschenfeldtMidwest Center for Structural Genomics, Argonne National Laboratory, Lemont, IL, USA.
Nicholas G WilsonDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.ORCID http://orcid.org/0000-0001-5158-2539
Jesse S BasraDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.ORCID http://orcid.org/0000-0003-4925-2543
Ricardo CortesDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.ORCID http://orcid.org/0000-0002-3225-2697
Zainab NoorsherDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
Youssef GabraielDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
Isaac Poonen-HonigDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.ORCID http://orcid.org/0000-0002-1847-0380
Elizabeth C SeacordDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
Celia W GouldingDepartment of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.ORCID http://orcid.org/0000-0001-5582-0565
David A LowBiomolecular Science and Engineering Program, University of California, Santa Barbara, CA, USA.ORCID http://orcid.org/0000-0002-8311-8244
Andrzej JoachimiakMidwest Center for Structural Genomics, Argonne National Laboratory, Lemont, IL, USA.ORCID http://orcid.org/0000-0003-2535-6209
Frederick W DahlquistDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
Christopher S HayesBiomolecular Science and Engineering Program, University of California, Santa Barbara, CA, USA. chayes@lifesci.ucsb.edu.ORCID http://orcid.org/0000-0002-2216-6445
University of California, Santa Barbara · USArgonne National Laboratory · USUniversity of California, Irvine · US

Funding

Molecular Mechanisms of anti-bacterial contact-dependent growth inhibition (CDI)R01GM117930 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI HAYES, CHRISTOPHER S. · 2016 to 2023
$3.0M
The Midwest Center for Structural Genomics - Community ResourceR24GM115586 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2015 to 2017
$2.8M
Structure-function analysis of polymorphic CDI toxin-immunity protein complexes aU01GM102318 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI GOULDING, CELIA · 2012 to 2016
$1.7M
Specificity Determinants of Contact Dependent InhibitionR21AI121789 · NIAID · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI DAHLQUIST, FREDERICK W. · 2016 to 2017
$386k
NIAID NIH HHS HHSN272201700060CNIAID NIH HHS R21 AI121789NIGMS NIH HHS R01 GM117930NIGMS NIH HHS R24 GM115586NIGMS NIH HHS U01 GM102318
6 · The paper itself

Abstract

Many Gram-negative bacteria use CdiA effector proteins to inhibit the growth of neighboring competitors. CdiA transfers its toxic CdiA-CT region into the periplasm of target cells, where it is released through proteolytic cleavage. The N-terminal cytoplasm-entry domain of the CdiA-CT then mediates translocation across the inner membrane to deliver the C-terminal toxin domain into the cytosol. Here, we show that proteolysis not only liberates the CdiA-CT for delivery, but is also required to activate the entry domain for membrane translocation. Translocation function depends on precise cleavage after a conserved VENN peptide sequence, and the processed ∆VENN entry domain exhibits distinct biophysical and thermodynamic properties. By contrast, imprecisely processed CdiA-CT fragments do not undergo this transition and fail to translocate to the cytoplasm. These findings suggest that CdiA-CT processing induces a critical structural switch that converts the entry domain into a membrane-translocation competent conformation.

Indexed as

Escherichia coli ProteinsAnti-Bacterial AgentsEscherichia coliMembrane ProteinsProteolysisAnti-Bacterial AgentsCdiA protein, E coliEscherichia coli ProteinsMembrane Proteins

Identifiers

PMID36038560
PMCPMC9424206
OpenAlexW4293475757

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.