Evidence map›Paper›PMID 26683375›Full record

ArticleThe Journal of biological chemistry2016

Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product.

Matthew Dunne, Stefan Leicht, Boris Krichel, Haydyn D T Mertens, Andrew Thompson, Jeroen Krijgsveld, Dmitri I Svergun, Natalia Gómez-Torres, Sonia Garde, Charlotte Uetrecht and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 45 citations in OpenAlex.

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  13. Novel Lytic Enzyme of Prophage Origin fromInternational journal of molecular sciences · 2021
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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

13 authors at 6 institutions in 4 countries.

Matthew DunneFrom the European Molecular Biology Laboratory, Notkestrasse 85, 22607 Hamburg, Germany.
Stefan Leichtthe European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Boris Krichelthe Heinrich Pette Institute, Leibniz Institute for Experimental Virology, Martinistrasse 52, 20251 Hamburg, Germany.
Haydyn D T MertensFrom the European Molecular Biology Laboratory, Notkestrasse 85, 22607 Hamburg, Germany.ORCID http://orcid.org/0000-0002-5664-744X
Andrew Thompsonthe Synchrotron Soleil, L'Orme des Merisiers, BP 48, Saint Aubin, 91192 Gif sur Yvette, France.
Jeroen Krijgsveldthe European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.ORCID http://orcid.org/0000-0001-7549-9326
Dmitri I SvergunFrom the European Molecular Biology Laboratory, Notkestrasse 85, 22607 Hamburg, Germany.ORCID http://orcid.org/0000-0003-0830-5696
Natalia Gómez-Torresthe Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, Departamento de Tecnología de Alimentos, Carretera de La Coruña km 7, 28040 Madrid, Spain.
Sonia Gardethe Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, Departamento de Tecnología de Alimentos, Carretera de La Coruña km 7, 28040 Madrid, Spain.
Charlotte Uetrechtthe Heinrich Pette Institute, Leibniz Institute for Experimental Virology, Martinistrasse 52, 20251 Hamburg, Germany, the European XFEL GmbH, Notkestrasse 85, 22607 Hamburg, Germany, and.ORCID http://orcid.org/0000-0002-1991-7922
Arjan Narbadthe Institute of Food Research, Colney, Norwich NR4 7UA, United Kingdom.
Melinda J Mayerthe Institute of Food Research, Colney, Norwich NR4 7UA, United Kingdom melinda.mayer@ifr.ac.uk.
Rob MeijersFrom the European Molecular Biology Laboratory, Notkestrasse 85, 22607 Hamburg, Germany, r.meijers@embl-hamburg.de.ORCID http://orcid.org/0000-0003-2872-6279
European Molecular Biology Laboratory · DEEuropean Molecular Biology Laboratory · DEInstituto Nacional de Investigación y Tecnología Agraria y Alimentaria · ESLeibniz Institute of Virology (LIV) · DENorwich Research Park · GBSynchrotron soleil · FR

Funding

Biotechnology and Biological Sciences Research Council BB/J004529/1Biotechnology and Biological Sciences Research Council BBS/E/F/00044453
6 · The paper itself

Abstract

Bacteriophages produce endolysins, which lyse the bacterial host cell to release newly produced virions. The timing of lysis is regulated and is thought to involve the activation of a molecular switch. We present a crystal structure of the activated endolysin CTP1L that targets Clostridium tyrobutyricum, consisting of a complex between the full-length protein and an N-terminally truncated C-terminal cell wall binding domain (CBD). The truncated CBD is produced through an internal translation start site within the endolysin gene. Mutants affecting the internal translation site change the oligomeric state of the endolysin and reduce lytic activity. The activity can be modulated by reconstitution of the full-length endolysin-CBD complex with free CBD. The same oligomerization mechanism applies to the CD27L endolysin that targets Clostridium difficile and the CS74L endolysin that targets Clostridium sporogenes. When the CTP1L endolysin gene is introduced into the commensal bacterium Lactococcus lactis, the truncated CBD is also produced, showing that the alternative start codon can be used in other bacterial species. The identification of a translational switch affecting oligomerization presented here has implications for the design of effective endolysins for the treatment of bacterial infections.

Indexed as

Amino Acid SequenceBacteriophagesClostridium tyrobutyricumCodon, InitiatorEndopeptidasesMolecular Sequence DataMutationProtein BindingProtein MultimerizationCodon, InitiatorendolysinEndopeptidasesantimicrobialbacteriophageClostridiaendolysinenzyme catalysismass spectrometry (MS)native mass spectrometryoligomerizationprotein structuresecondary translation

Identifiers

PMID26683375
PMCPMC4777826
OpenAlexW2260374461

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.