A novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.

Manganese ions (Mn(2+)) play a crucial role in virulence and protection against oxidative stress in bacterial pathogens. Such pathogens appear to have evolved complex mechanisms for regulating Mn(2+) uptake and efflux. Despite numerous studies on Mn(2+) uptake, however, only one efflux system has be...

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Autores principales:	Chunxia Li, Jun Tao, Daqing Mao, Chaozu He
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3d0497238225461ca2266f044f8f992a
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spelling	oai:doaj.org-article:3d0497238225461ca2266f044f8f992a2021-11-18T06:50:13ZA novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.1932-620310.1371/journal.pone.0021983https://doaj.org/article/3d0497238225461ca2266f044f8f992a2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21789199/?tool=EBIhttps://doaj.org/toc/1932-6203Manganese ions (Mn(2+)) play a crucial role in virulence and protection against oxidative stress in bacterial pathogens. Such pathogens appear to have evolved complex mechanisms for regulating Mn(2+) uptake and efflux. Despite numerous studies on Mn(2+) uptake, however, only one efflux system has been identified to date. Here, we report on a novel Mn(2+) export system, YebN, in Xanthomonas oryzae pv. oryzae (Xoo), the causative agent of bacterial leaf blight. Compared with wild-type PXO99, the yebN mutant was highly sensitive to Mn(2+) and accumulated high concentrations of intracellular manganese. In addition, we found that expression of yebN was positively regulated by Mn(2+) and the Mn(2+)-dependent transcription regulator, MntR. Interestingly, the yebN mutant was more tolerant to methyl viologen and H(2)O(2) in low Mn(2+) medium than PXO99, but more sensitive in high Mn(2+) medium, implying that YebN plays an important role in Mn(2+) homoeostasis and detoxification of reactive oxygen species (ROS). Notably, deletion of yebN rendered Xoo sensitive to hypo-osmotic shock, suggesting that YebN may protect against such stress. That mutation of yebN substantially reduced the Xoo growth rate and lesion formation in rice implies that YebN could be involved in Xoo fitness in host. Although YebN has two DUF204 domains, it lacks homology to any known metal transporter. Hence, this is the first report of a novel metal export system that plays essential roles in hypo-osmotic and oxidative stress, and virulence. Our results lay the foundations for elucidating the complex and fascinating relationship between metal homeostasis and host-pathogen interactions.Chunxia LiJun TaoDaqing MaoChaozu HePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 7, p e21983 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chunxia Li Jun Tao Daqing Mao Chaozu He A novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.
description	Manganese ions (Mn(2+)) play a crucial role in virulence and protection against oxidative stress in bacterial pathogens. Such pathogens appear to have evolved complex mechanisms for regulating Mn(2+) uptake and efflux. Despite numerous studies on Mn(2+) uptake, however, only one efflux system has been identified to date. Here, we report on a novel Mn(2+) export system, YebN, in Xanthomonas oryzae pv. oryzae (Xoo), the causative agent of bacterial leaf blight. Compared with wild-type PXO99, the yebN mutant was highly sensitive to Mn(2+) and accumulated high concentrations of intracellular manganese. In addition, we found that expression of yebN was positively regulated by Mn(2+) and the Mn(2+)-dependent transcription regulator, MntR. Interestingly, the yebN mutant was more tolerant to methyl viologen and H(2)O(2) in low Mn(2+) medium than PXO99, but more sensitive in high Mn(2+) medium, implying that YebN plays an important role in Mn(2+) homoeostasis and detoxification of reactive oxygen species (ROS). Notably, deletion of yebN rendered Xoo sensitive to hypo-osmotic shock, suggesting that YebN may protect against such stress. That mutation of yebN substantially reduced the Xoo growth rate and lesion formation in rice implies that YebN could be involved in Xoo fitness in host. Although YebN has two DUF204 domains, it lacks homology to any known metal transporter. Hence, this is the first report of a novel metal export system that plays essential roles in hypo-osmotic and oxidative stress, and virulence. Our results lay the foundations for elucidating the complex and fascinating relationship between metal homeostasis and host-pathogen interactions.
format	article
author	Chunxia Li Jun Tao Daqing Mao Chaozu He
author_facet	Chunxia Li Jun Tao Daqing Mao Chaozu He
author_sort	Chunxia Li
title	A novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.
title_short	A novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.
title_full	A novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.
title_fullStr	A novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.
title_full_unstemmed	A novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.
title_sort	novel manganese efflux system, yebn, is required for virulence by xanthomonas oryzae pv. oryzae.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/3d0497238225461ca2266f044f8f992a
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A novel manganese efflux system, YebN, is required for virulence by Xanthomonas oryzae pv. oryzae.

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