treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity.
Citrus canker, caused by the bacterium Xanthomonas citri subsp. citri (Xcc), is a severe disease of citrus. Xcc presents broad spectrum of citrus hosts including economically important species whereas X. fuscans subsp. aurantifolii-type C (XauC) causes a milder disease and only infects Citrus aurant...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2016-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0162886 |
| _version_ | 1818678166978297856 |
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| author | André Vessoni Alexandrino Leandro Seiji Goto Maria Teresa Marques Novo-Mansur |
| author_facet | André Vessoni Alexandrino Leandro Seiji Goto Maria Teresa Marques Novo-Mansur |
| author_sort | André Vessoni Alexandrino |
| collection | DOAJ |
| description | Citrus canker, caused by the bacterium Xanthomonas citri subsp. citri (Xcc), is a severe disease of citrus. Xcc presents broad spectrum of citrus hosts including economically important species whereas X. fuscans subsp. aurantifolii-type C (XauC) causes a milder disease and only infects Citrus aurantifolia. Trehalase catalyzes hydrolysis of the disaccharide trehalose, a sugar that has been reported to be related to Xcc pathogenicity. We expressed the recombinant gene product and assessed Xcc trehalase structural and kinetics data. The recombinant protein presented 42.7% of secondary structures in α-helix and 13% in β-sheets, no quaternary structure in solution, and Michaelis-Menten constant (KM) of 0.077 mM and Vmax 55.308 μMol glucose.min-1.mg protein-1 for trehalose. A Xcc mutant strain (XccΔtreA) was produced by gene deletion from Xcc genome. Enzymatic activity of trehalase was determined in Xcc, XauC and XccΔtreA cellular lysates, showing the highest values for XauC in in vitro infective condition and no activity for XccΔtreA. Finally, leaves of Citrus aurantifolia infected with XccΔtreA showed much more drenching and necrosis than those infected by wild type Xcc. We concluded that trehalase contributes to alleviate bacterial virulence and that inability for trehalose hydrolysis may promote higher Xcc infectivity. |
| first_indexed | 2024-12-17T09:10:57Z |
| format | Article |
| id | doaj.art-92f82b690ce64242bcff55f34b07b3b3 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-17T09:10:57Z |
| publishDate | 2016-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-92f82b690ce64242bcff55f34b07b3b32022-12-21T21:55:12ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01119e016288610.1371/journal.pone.0162886treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity.André Vessoni AlexandrinoLeandro Seiji GotoMaria Teresa Marques Novo-MansurCitrus canker, caused by the bacterium Xanthomonas citri subsp. citri (Xcc), is a severe disease of citrus. Xcc presents broad spectrum of citrus hosts including economically important species whereas X. fuscans subsp. aurantifolii-type C (XauC) causes a milder disease and only infects Citrus aurantifolia. Trehalase catalyzes hydrolysis of the disaccharide trehalose, a sugar that has been reported to be related to Xcc pathogenicity. We expressed the recombinant gene product and assessed Xcc trehalase structural and kinetics data. The recombinant protein presented 42.7% of secondary structures in α-helix and 13% in β-sheets, no quaternary structure in solution, and Michaelis-Menten constant (KM) of 0.077 mM and Vmax 55.308 μMol glucose.min-1.mg protein-1 for trehalose. A Xcc mutant strain (XccΔtreA) was produced by gene deletion from Xcc genome. Enzymatic activity of trehalase was determined in Xcc, XauC and XccΔtreA cellular lysates, showing the highest values for XauC in in vitro infective condition and no activity for XccΔtreA. Finally, leaves of Citrus aurantifolia infected with XccΔtreA showed much more drenching and necrosis than those infected by wild type Xcc. We concluded that trehalase contributes to alleviate bacterial virulence and that inability for trehalose hydrolysis may promote higher Xcc infectivity.https://doi.org/10.1371/journal.pone.0162886 |
| spellingShingle | André Vessoni Alexandrino Leandro Seiji Goto Maria Teresa Marques Novo-Mansur treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity. PLoS ONE |
| title | treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity. |
| title_full | treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity. |
| title_fullStr | treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity. |
| title_full_unstemmed | treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity. |
| title_short | treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity. |
| title_sort | trea codifies for a trehalase with involvement in xanthomonas citri subsp citri pathogenicity |
| url | https://doi.org/10.1371/journal.pone.0162886 |
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