Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides

The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide the first structural evidence on the recognition mechanism and our biochemical data show that another closely related lasso peptide cannot interact with FhuA. Our work pro...

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Autores principales: Mathavan, Indran, Zirah, Séverine, Mehmood, Shahid, Choudhury, Hassanul G., Goulard, Christophe, Li, Yanyan, Robinson, Carol V., Rebuffat, Sylvie, Beis, Konstantinos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3992131/
https://www.ncbi.nlm.nih.gov/pubmed/24705590
http://dx.doi.org/10.1038/nchembio.1499
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author Mathavan, Indran
Zirah, Séverine
Mehmood, Shahid
Choudhury, Hassanul G.
Goulard, Christophe
Li, Yanyan
Robinson, Carol V.
Rebuffat, Sylvie
Beis, Konstantinos
author_facet Mathavan, Indran
Zirah, Séverine
Mehmood, Shahid
Choudhury, Hassanul G.
Goulard, Christophe
Li, Yanyan
Robinson, Carol V.
Rebuffat, Sylvie
Beis, Konstantinos
author_sort Mathavan, Indran
collection PubMed
description The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide the first structural evidence on the recognition mechanism and our biochemical data show that another closely related lasso peptide cannot interact with FhuA. Our work provides an explanation on the narrow activity spectrum of lasso peptides and opens the path to the development of new antibacterials.
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spelling pubmed-39921312014-11-01 Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides Mathavan, Indran Zirah, Séverine Mehmood, Shahid Choudhury, Hassanul G. Goulard, Christophe Li, Yanyan Robinson, Carol V. Rebuffat, Sylvie Beis, Konstantinos Nat Chem Biol Article The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide the first structural evidence on the recognition mechanism and our biochemical data show that another closely related lasso peptide cannot interact with FhuA. Our work provides an explanation on the narrow activity spectrum of lasso peptides and opens the path to the development of new antibacterials. 2014-04-06 2014-05 /pmc/articles/PMC3992131/ /pubmed/24705590 http://dx.doi.org/10.1038/nchembio.1499 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Mathavan, Indran
Zirah, Séverine
Mehmood, Shahid
Choudhury, Hassanul G.
Goulard, Christophe
Li, Yanyan
Robinson, Carol V.
Rebuffat, Sylvie
Beis, Konstantinos
Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
title Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
title_full Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
title_fullStr Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
title_full_unstemmed Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
title_short Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
title_sort structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3992131/
https://www.ncbi.nlm.nih.gov/pubmed/24705590
http://dx.doi.org/10.1038/nchembio.1499
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