Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis
Polysaccharide (PS) capsules are important virulence determinants for many bacterial pathogens. Bordetella pertussis, the agent of whooping cough, produces a surface associated microcapsule but its role in pertussis pathogenesis remained unknown. Here we showed that the B. pertussis capsule locus is...
| Main Authors: | , , , , , , |
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| Format: | Journal Article |
| Language: | English |
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2015
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| Online Access: | https://hdl.handle.net/10356/104381 http://hdl.handle.net/10220/24600 |
| _version_ | 1826125927763935232 |
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| author | Hoo, Regina Lam, Jian Hang Huot, Ludovic Pant, Aakanksha Li, Rui Hot, David Alonso, Sylvie |
| author2 | Hozbor, Daniela Flavia |
| author_facet | Hozbor, Daniela Flavia Hoo, Regina Lam, Jian Hang Huot, Ludovic Pant, Aakanksha Li, Rui Hot, David Alonso, Sylvie |
| author_sort | Hoo, Regina |
| collection | NTU |
| description | Polysaccharide (PS) capsules are important virulence determinants for many bacterial pathogens. Bordetella pertussis, the agent of whooping cough, produces a surface associated microcapsule but its role in pertussis pathogenesis remained unknown. Here we showed that the B. pertussis capsule locus is expressed in vivo in murine lungs and that absence of the membrane-associated protein KpsT, involved in the transport of the PS polymers across the envelope, but not the surface-exposed PS capsule itself, affects drastically B. pertussis colonization efficacy in mice. Microarray analysis revealed that absence of KpsT in B. pertussis resulted in global down-regulation of gene expression including key virulence genes regulated by BvgA/S, the master two-component system. Using a BvgS phase-locked mutant, we demonstrated a functional link between KpsT and BvgA/S-mediated signal transduction. Whereas pull-down assays do not support physical interaction between BvgS sensor and any of the capsule locus encoded proteins, absence of KpsT impaired BvgS oligomerization, necessary for BvgS function. Furthermore, complementation studies indicated that instead of KpsT alone, the entire PS capsule transport machinery spanning the cell envelope likely plays a role in BvgS-mediated signal transduction. Our work thus provides the first experimental evidence of a role for a virulence-repressed gene in pertussis pathogenesis. |
| first_indexed | 2024-10-01T06:44:23Z |
| format | Journal Article |
| id | ntu-10356/104381 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:44:23Z |
| publishDate | 2015 |
| record_format | dspace |
| spelling | ntu-10356/1043812023-02-28T17:06:15Z Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis Hoo, Regina Lam, Jian Hang Huot, Ludovic Pant, Aakanksha Li, Rui Hot, David Alonso, Sylvie Hozbor, Daniela Flavia School of Biological Sciences DRNTU::Science::Biological sciences::Microbiology::Bacteria Polysaccharide (PS) capsules are important virulence determinants for many bacterial pathogens. Bordetella pertussis, the agent of whooping cough, produces a surface associated microcapsule but its role in pertussis pathogenesis remained unknown. Here we showed that the B. pertussis capsule locus is expressed in vivo in murine lungs and that absence of the membrane-associated protein KpsT, involved in the transport of the PS polymers across the envelope, but not the surface-exposed PS capsule itself, affects drastically B. pertussis colonization efficacy in mice. Microarray analysis revealed that absence of KpsT in B. pertussis resulted in global down-regulation of gene expression including key virulence genes regulated by BvgA/S, the master two-component system. Using a BvgS phase-locked mutant, we demonstrated a functional link between KpsT and BvgA/S-mediated signal transduction. Whereas pull-down assays do not support physical interaction between BvgS sensor and any of the capsule locus encoded proteins, absence of KpsT impaired BvgS oligomerization, necessary for BvgS function. Furthermore, complementation studies indicated that instead of KpsT alone, the entire PS capsule transport machinery spanning the cell envelope likely plays a role in BvgS-mediated signal transduction. Our work thus provides the first experimental evidence of a role for a virulence-repressed gene in pertussis pathogenesis. Published version 2015-01-14T02:59:51Z 2019-12-06T21:31:39Z 2015-01-14T02:59:51Z 2019-12-06T21:31:39Z 2014 2014 Journal Article Hoo, R., Lam, J. H., Huot, L., Pant, A., Li, R., Hot, D., et al. (2014). Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis. PLoS One, 9(12), e115243-. 1932-6203 https://hdl.handle.net/10356/104381 http://hdl.handle.net/10220/24600 10.1371/journal.pone.0115243 25501560 en PLoS One © 2014 Hoo et al. 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 credited. application/pdf |
| spellingShingle | DRNTU::Science::Biological sciences::Microbiology::Bacteria Hoo, Regina Lam, Jian Hang Huot, Ludovic Pant, Aakanksha Li, Rui Hot, David Alonso, Sylvie Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis |
| title | Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis |
| title_full | Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis |
| title_fullStr | Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis |
| title_full_unstemmed | Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis |
| title_short | Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis |
| title_sort | evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis |
| topic | DRNTU::Science::Biological sciences::Microbiology::Bacteria |
| url | https://hdl.handle.net/10356/104381 http://hdl.handle.net/10220/24600 |
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