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Role of the FnIII domain associated with a cell wall‐degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae
Cellobiosidase (CbsA) is an important secreted virulence factor of Xanthomonas oryzae pv. oryzae (Xoo), which causes bacterial blight of rice. CbsA is one of several cell wall‐degrading enzymes secreted by Xoo via the type II secretion system (T2SS). CbsA is considered a fundamental virulence factor...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9190976/ https://www.ncbi.nlm.nih.gov/pubmed/35278018 http://dx.doi.org/10.1111/mpp.13205 |
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author | Nathawat, Rajkanwar Maku, Roshan V. Patel, Hitendra K. Sankaranarayanan, Rajan Sonti, Ramesh V. |
author_facet | Nathawat, Rajkanwar Maku, Roshan V. Patel, Hitendra K. Sankaranarayanan, Rajan Sonti, Ramesh V. |
author_sort | Nathawat, Rajkanwar |
collection | PubMed |
description | Cellobiosidase (CbsA) is an important secreted virulence factor of Xanthomonas oryzae pv. oryzae (Xoo), which causes bacterial blight of rice. CbsA is one of several cell wall‐degrading enzymes secreted by Xoo via the type II secretion system (T2SS). CbsA is considered a fundamental virulence factor for vascular pathogenesis. CbsA has an N‐terminal glycosyl hydrolase domain and a C‐terminal fibronectin type III (FnIII) domain. Interestingly, the secreted form of CbsA lacks the FnIII domain during in planta growth. Here we show that the presence of the FnIII domain inhibits the enzyme activity of CbsA on polysaccharide substrates like carboxymethylcellulose. The FnIII domain is required for the interaction of CbsA with SecB chaperone, and this interaction is crucial for the stability and efficient transport of CbsA across the inner membrane. Deletion of the FnIII domain reduced virulence similar to ΔcbsA Xoo, which corroborates the importance of the FnIII domain in CbsA. Our work elucidates a hitherto unknown function of the FnIII domain in enabling the virulence‐promoting activity of CbsA. |
format | Online Article Text |
id | pubmed-9190976 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-91909762022-06-21 Role of the FnIII domain associated with a cell wall‐degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae Nathawat, Rajkanwar Maku, Roshan V. Patel, Hitendra K. Sankaranarayanan, Rajan Sonti, Ramesh V. Mol Plant Pathol Original Articles Cellobiosidase (CbsA) is an important secreted virulence factor of Xanthomonas oryzae pv. oryzae (Xoo), which causes bacterial blight of rice. CbsA is one of several cell wall‐degrading enzymes secreted by Xoo via the type II secretion system (T2SS). CbsA is considered a fundamental virulence factor for vascular pathogenesis. CbsA has an N‐terminal glycosyl hydrolase domain and a C‐terminal fibronectin type III (FnIII) domain. Interestingly, the secreted form of CbsA lacks the FnIII domain during in planta growth. Here we show that the presence of the FnIII domain inhibits the enzyme activity of CbsA on polysaccharide substrates like carboxymethylcellulose. The FnIII domain is required for the interaction of CbsA with SecB chaperone, and this interaction is crucial for the stability and efficient transport of CbsA across the inner membrane. Deletion of the FnIII domain reduced virulence similar to ΔcbsA Xoo, which corroborates the importance of the FnIII domain in CbsA. Our work elucidates a hitherto unknown function of the FnIII domain in enabling the virulence‐promoting activity of CbsA. John Wiley and Sons Inc. 2022-03-12 /pmc/articles/PMC9190976/ /pubmed/35278018 http://dx.doi.org/10.1111/mpp.13205 Text en © 2022 The Authors. Molecular Plant Pathology published by British Society for Plant Pathology and John Wiley & Sons Ltd. https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Original Articles Nathawat, Rajkanwar Maku, Roshan V. Patel, Hitendra K. Sankaranarayanan, Rajan Sonti, Ramesh V. Role of the FnIII domain associated with a cell wall‐degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae |
title | Role of the FnIII domain associated with a cell wall‐degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae
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title_full | Role of the FnIII domain associated with a cell wall‐degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae
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title_fullStr | Role of the FnIII domain associated with a cell wall‐degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae
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title_full_unstemmed | Role of the FnIII domain associated with a cell wall‐degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae
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title_short | Role of the FnIII domain associated with a cell wall‐degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae
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title_sort | role of the fniii domain associated with a cell wall‐degrading enzyme cellobiosidase of xanthomonas oryzae pv. oryzae |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9190976/ https://www.ncbi.nlm.nih.gov/pubmed/35278018 http://dx.doi.org/10.1111/mpp.13205 |
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