Flagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level

Abstract Host-microbe interactions determine the outcome of host responses to commensal and pathogenic microbes. Previously, two epithelial cell-binding peptides were found to be homologues of two sites (B, aa168–174; F, aa303–309) in the flagellar hook protein FlgE of Pseudomonas aeruginosa. Tertia...

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Autores principales:	Ying Shen, Lin Chen, Meixiang Wang, Dandan Lin, Zhongjie Liang, Peiqing Song, Qing Yuan, Hua Tang, Weihua Li, Kangmin Duan, Baiyan Liu, Ge Zhao, Yiqiang Wang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7ebbf896e5934f6cb3c71d42c3319adf
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spelling	oai:doaj.org-article:7ebbf896e5934f6cb3c71d42c3319adf2021-12-02T16:06:32ZFlagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level10.1038/s41598-017-01619-12045-2322https://doaj.org/article/7ebbf896e5934f6cb3c71d42c3319adf2017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01619-1https://doaj.org/toc/2045-2322Abstract Host-microbe interactions determine the outcome of host responses to commensal and pathogenic microbes. Previously, two epithelial cell-binding peptides were found to be homologues of two sites (B, aa168–174; F, aa303–309) in the flagellar hook protein FlgE of Pseudomonas aeruginosa. Tertiary modeling predicted these sites at the interface of neighboring FlgE monomers in the fully formed hook. Recombinant FlgE protein stimulated proinflammatory cytokine production in a human cell line and in murine lung organoid culture as detected with real-time RT-PCR and ELISA assays. When administered to mice, FlgE induced lung inflammation and enhanced the Th2-biased humoral response to ovalbumin. A pull-down assay performed with FlgE-saturated resin identified caveolin-1 as an FlgE-binding protein, and caveolin-1 deficiency impaired FlgE-induced inflammation and downstream Erk1/2 pathway activation in lung organoids. Intact flagellar hooks from bacteria were also proinflammatory. Mutations to sites B and F impaired bacteria motility and proinflammatory potency of FlgE without altering adjuvanticity of FlgE. These findings suggest that the flagellar hook and FlgE are novel players in host-bacterial interactions at immunological level. Further studies along this direction would provide new opportunities for understanding and management of diseases related with bacterial infection.Ying ShenLin ChenMeixiang WangDandan LinZhongjie LiangPeiqing SongQing YuanHua TangWeihua LiKangmin DuanBaiyan LiuGe ZhaoYiqiang WangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ying Shen Lin Chen Meixiang Wang Dandan Lin Zhongjie Liang Peiqing Song Qing Yuan Hua Tang Weihua Li Kangmin Duan Baiyan Liu Ge Zhao Yiqiang Wang Flagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level
description	Abstract Host-microbe interactions determine the outcome of host responses to commensal and pathogenic microbes. Previously, two epithelial cell-binding peptides were found to be homologues of two sites (B, aa168–174; F, aa303–309) in the flagellar hook protein FlgE of Pseudomonas aeruginosa. Tertiary modeling predicted these sites at the interface of neighboring FlgE monomers in the fully formed hook. Recombinant FlgE protein stimulated proinflammatory cytokine production in a human cell line and in murine lung organoid culture as detected with real-time RT-PCR and ELISA assays. When administered to mice, FlgE induced lung inflammation and enhanced the Th2-biased humoral response to ovalbumin. A pull-down assay performed with FlgE-saturated resin identified caveolin-1 as an FlgE-binding protein, and caveolin-1 deficiency impaired FlgE-induced inflammation and downstream Erk1/2 pathway activation in lung organoids. Intact flagellar hooks from bacteria were also proinflammatory. Mutations to sites B and F impaired bacteria motility and proinflammatory potency of FlgE without altering adjuvanticity of FlgE. These findings suggest that the flagellar hook and FlgE are novel players in host-bacterial interactions at immunological level. Further studies along this direction would provide new opportunities for understanding and management of diseases related with bacterial infection.
format	article
author	Ying Shen Lin Chen Meixiang Wang Dandan Lin Zhongjie Liang Peiqing Song Qing Yuan Hua Tang Weihua Li Kangmin Duan Baiyan Liu Ge Zhao Yiqiang Wang
author_facet	Ying Shen Lin Chen Meixiang Wang Dandan Lin Zhongjie Liang Peiqing Song Qing Yuan Hua Tang Weihua Li Kangmin Duan Baiyan Liu Ge Zhao Yiqiang Wang
author_sort	Ying Shen
title	Flagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level
title_short	Flagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level
title_full	Flagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level
title_fullStr	Flagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level
title_full_unstemmed	Flagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level
title_sort	flagellar hooks and hook protein flge participate in host microbe interactions at immunological level
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/7ebbf896e5934f6cb3c71d42c3319adf
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_version_	1718384971669831680

Flagellar Hooks and Hook Protein FlgE Participate in Host Microbe Interactions at Immunological Level

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