Small Protein-Mediated Quorum Sensing in a Gram-Negative Bacterium

The rice XA21 pattern recognition receptor binds a type I secreted sulfated peptide, called axY(S)22, derived from the Ax21 (activator of XA21-mediated immunity) protein. The conservation of Ax21 in all sequenced Xanthomonas spp. and closely related genera suggests that Ax21 serves a key biological...

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Autores principales: Han, Sang-Wook, Sriariyanun, Malinee, Lee, Sang-Won, Sharma, Manoj, Bahar, Ofir, Bower, Zachary, Ronald, Pamela C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3236232/
https://www.ncbi.nlm.nih.gov/pubmed/22174954
http://dx.doi.org/10.1371/journal.pone.0029192
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author Han, Sang-Wook
Sriariyanun, Malinee
Lee, Sang-Won
Sharma, Manoj
Bahar, Ofir
Bower, Zachary
Ronald, Pamela C.
author_facet Han, Sang-Wook
Sriariyanun, Malinee
Lee, Sang-Won
Sharma, Manoj
Bahar, Ofir
Bower, Zachary
Ronald, Pamela C.
author_sort Han, Sang-Wook
collection PubMed
description The rice XA21 pattern recognition receptor binds a type I secreted sulfated peptide, called axY(S)22, derived from the Ax21 (activator of XA21-mediated immunity) protein. The conservation of Ax21 in all sequenced Xanthomonas spp. and closely related genera suggests that Ax21 serves a key biological function. Here we show that the predicted N-terminal sequence of Ax21 is cleaved prior to secretion outside the cell and that mature Ax21 serves as a quorum sensing (QS) factor in Xanthomonas oryzae pv. oryzae. Ax21-mediated QS controls motility, biofilm formation and virulence. We provide genetic evidence that the Xoo RaxH histidine kinase serves as the bacterial receptor for Ax21. This work establishes a critical role for small protein-mediated QS in a Gram-negative bacterium.
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spelling pubmed-32362322011-12-15 Small Protein-Mediated Quorum Sensing in a Gram-Negative Bacterium Han, Sang-Wook Sriariyanun, Malinee Lee, Sang-Won Sharma, Manoj Bahar, Ofir Bower, Zachary Ronald, Pamela C. PLoS One Research Article The rice XA21 pattern recognition receptor binds a type I secreted sulfated peptide, called axY(S)22, derived from the Ax21 (activator of XA21-mediated immunity) protein. The conservation of Ax21 in all sequenced Xanthomonas spp. and closely related genera suggests that Ax21 serves a key biological function. Here we show that the predicted N-terminal sequence of Ax21 is cleaved prior to secretion outside the cell and that mature Ax21 serves as a quorum sensing (QS) factor in Xanthomonas oryzae pv. oryzae. Ax21-mediated QS controls motility, biofilm formation and virulence. We provide genetic evidence that the Xoo RaxH histidine kinase serves as the bacterial receptor for Ax21. This work establishes a critical role for small protein-mediated QS in a Gram-negative bacterium. Public Library of Science 2011-12-12 /pmc/articles/PMC3236232/ /pubmed/22174954 http://dx.doi.org/10.1371/journal.pone.0029192 Text en Han et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Han, Sang-Wook
Sriariyanun, Malinee
Lee, Sang-Won
Sharma, Manoj
Bahar, Ofir
Bower, Zachary
Ronald, Pamela C.
Small Protein-Mediated Quorum Sensing in a Gram-Negative Bacterium
title Small Protein-Mediated Quorum Sensing in a Gram-Negative Bacterium
title_full Small Protein-Mediated Quorum Sensing in a Gram-Negative Bacterium
title_fullStr Small Protein-Mediated Quorum Sensing in a Gram-Negative Bacterium
title_full_unstemmed Small Protein-Mediated Quorum Sensing in a Gram-Negative Bacterium
title_short Small Protein-Mediated Quorum Sensing in a Gram-Negative Bacterium
title_sort small protein-mediated quorum sensing in a gram-negative bacterium
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3236232/
https://www.ncbi.nlm.nih.gov/pubmed/22174954
http://dx.doi.org/10.1371/journal.pone.0029192
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