Mannitol metabolism during pathogenic fungal–host interactions under stressed conditions
Identifieur interne : 000626 ( Ncbi/Merge ); précédent : 000625; suivant : 000627Mannitol metabolism during pathogenic fungal–host interactions under stressed conditions
Auteurs : Mukesh Meena [Inde] ; Vishal Prasad [Inde] ; Andleeb Zehra [Inde] ; Vijai K. Gupta [Irlande (pays)] ; Ram S. Upadhyay [Inde]Source :
- Frontiers in Microbiology [ 1664-302X ] ; 2015.
Abstract
Numerous plants and fungi produce mannitol, which may serve as an osmolyte or metabolic store; furthermore, mannitol also acts as a powerful quencher of reactive oxygen species (ROS). Some phytopathogenic fungi use mannitol to stifle ROS-mediated plant resistance. Mannitol is essential in pathogenesis to balance cell reinforcements produced by both plants and animals. Mannitol likewise serves as a source of reducing power, managing coenzymes, and controlling cytoplasmic pH by going about as a sink or hotspot for protons. The metabolic pathways for mannitol biosynthesis and catabolism have been characterized in filamentous fungi by direct diminishment of fructose-6-phosphate into mannitol-1-phosphate including a mannitol-1-phosphate phosphatase catalyst. In plants mannitol is integrated from mannose-6-phosphate to mannitol-1-phosphate, which then dephosphorylates to mannitol. The enzyme mannitol dehydrogenase plays a key role in host–pathogen interactions and must be co-localized with pathogen-secreted mannitol to resist the infection.
Url:
DOI: 10.3389/fmicb.2015.01019
PubMed: 26441941
PubMed Central: 4585237
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<front><div type="abstract" xml:lang="en"><p>Numerous plants and fungi produce mannitol, which may serve as an osmolyte or metabolic store; furthermore, mannitol also acts as a powerful quencher of reactive oxygen species (ROS). Some phytopathogenic fungi use mannitol to stifle ROS-mediated plant resistance. Mannitol is essential in pathogenesis to balance cell reinforcements produced by both plants and animals. Mannitol likewise serves as a source of reducing power, managing coenzymes, and controlling cytoplasmic pH by going about as a sink or hotspot for protons. The metabolic pathways for mannitol biosynthesis and catabolism have been characterized in filamentous fungi by direct diminishment of fructose-6-phosphate into mannitol-1-phosphate including a mannitol-1-phosphate phosphatase catalyst. In plants mannitol is integrated from mannose-6-phosphate to mannitol-1-phosphate, which then dephosphorylates to mannitol. The enzyme mannitol dehydrogenase plays a key role in host–pathogen interactions and must be co-localized with pathogen-secreted mannitol to resist the infection.</p>
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<pmc article-type="review-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Front Microbiol</journal-id>
<journal-id journal-id-type="iso-abbrev">Front Microbiol</journal-id>
<journal-id journal-id-type="publisher-id">Front. Microbiol.</journal-id>
<journal-title-group><journal-title>Frontiers in Microbiology</journal-title>
</journal-title-group>
<issn pub-type="epub">1664-302X</issn>
<publisher><publisher-name>Frontiers Media S.A.</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">26441941</article-id>
<article-id pub-id-type="pmc">4585237</article-id>
<article-id pub-id-type="doi">10.3389/fmicb.2015.01019</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Microbiology</subject>
<subj-group><subject>Review</subject>
</subj-group>
</subj-group>
</article-categories>
<title-group><article-title>Mannitol metabolism during pathogenic fungal–host interactions under stressed conditions</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Meena</surname>
<given-names>Mukesh</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
<uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/232105/overview"></uri>
</contrib>
<contrib contrib-type="author"><name><surname>Prasad</surname>
<given-names>Vishal</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zehra</surname>
<given-names>Andleeb</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Gupta</surname>
<given-names>Vijai K.</given-names>
</name>
<xref ref-type="aff" rid="aff3"><sup>3</sup>
</xref>
<uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/177156/overview"></uri>
</contrib>
<contrib contrib-type="author"><name><surname>Upadhyay</surname>
<given-names>Ram S.</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
<xref ref-type="author-notes" rid="fn001"><sup>*</sup>
</xref>
<uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/237209/overview"></uri>
</contrib>
</contrib-group>
<aff id="aff1"><sup>1</sup>
<institution>Department of Botany, Banaras Hindu University</institution>
<country>Varanasi, India</country>
</aff>
<aff id="aff2"><sup>2</sup>
<institution>Institute of Environment and Sustainable Development, Banaras Hindu University</institution>
<country>Varanasi, India</country>
</aff>
<aff id="aff3"><sup>3</sup>
<institution>Molecular Glycobiotechnology Group, Discipline of Biochemistry, School of Natural Sciences, National University of Ireland Galway</institution>
<country>Galway, Ireland</country>
</aff>
<author-notes><fn fn-type="edited-by"><p>Edited by: <italic>Simone Ferrari, Sapienza Università di Roma, Italy</italic>
</p>
</fn>
<fn fn-type="edited-by"><p>Reviewed by: <italic>Anthonia O’Donovan, Technology Centre Biofuel and Biorefinery, Ireland; Hesham Ali El-Enshasy, Universiti Teknologi Malaysia, Malaysia</italic>
</p>
</fn>
<corresp id="fn001">*Correspondence: <italic>Ram S. Upadhyay, Department of Botany, Banaras Hindu University, Varanasi 221 005, India, <email xlink:type="simple">upadhyay_bhu@yahoo.co.uk</email>
; <email xlink:type="simple">upadhyay.bot@gmail.com</email>
</italic>
</corresp>
<fn fn-type="other" id="fn002"><p>This article was submitted to Plant Biotic Interactions, a section of the journal Frontiers in Microbiology</p>
</fn>
</author-notes>
<pub-date pub-type="epub"><day>24</day>
<month>9</month>
<year>2015</year>
</pub-date>
<pub-date pub-type="collection"><year>2015</year>
</pub-date>
<volume>6</volume>
<elocation-id>1019</elocation-id>
<history><date date-type="received"><day>06</day>
<month>8</month>
<year>2015</year>
</date>
<date date-type="accepted"><day>08</day>
<month>9</month>
<year>2015</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2015 Meena, Prasad, Zehra, Gupta and Upadhyay.</copyright-statement>
<copyright-year>2015</copyright-year>
<copyright-holder>Meena, Prasad, Zehra, Gupta and Upadhyay</copyright-holder>
<license xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.</license-p>
</license>
</permissions>
<abstract><p>Numerous plants and fungi produce mannitol, which may serve as an osmolyte or metabolic store; furthermore, mannitol also acts as a powerful quencher of reactive oxygen species (ROS). Some phytopathogenic fungi use mannitol to stifle ROS-mediated plant resistance. Mannitol is essential in pathogenesis to balance cell reinforcements produced by both plants and animals. Mannitol likewise serves as a source of reducing power, managing coenzymes, and controlling cytoplasmic pH by going about as a sink or hotspot for protons. The metabolic pathways for mannitol biosynthesis and catabolism have been characterized in filamentous fungi by direct diminishment of fructose-6-phosphate into mannitol-1-phosphate including a mannitol-1-phosphate phosphatase catalyst. In plants mannitol is integrated from mannose-6-phosphate to mannitol-1-phosphate, which then dephosphorylates to mannitol. The enzyme mannitol dehydrogenase plays a key role in host–pathogen interactions and must be co-localized with pathogen-secreted mannitol to resist the infection.</p>
</abstract>
<kwd-group><kwd>Mannitol</kwd>
<kwd>reactive oxygen species (ROS)</kwd>
<kwd>mannitol dehydrogenase (MTD)</kwd>
<kwd>mannitol-1-phosphate-5-dehydrogenase (MPD)</kwd>
<kwd>polyols</kwd>
</kwd-group>
<counts><fig-count count="3"></fig-count>
<table-count count="1"></table-count>
<equation-count count="0"></equation-count>
<ref-count count="114"></ref-count>
<page-count count="12"></page-count>
<word-count count="0"></word-count>
</counts>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>Inde</li>
<li>Irlande (pays)</li>
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<tree><country name="Inde"><noRegion><name sortKey="Meena, Mukesh" sort="Meena, Mukesh" uniqKey="Meena M" first="Mukesh" last="Meena">Mukesh Meena</name>
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<name sortKey="Upadhyay, Ram S" sort="Upadhyay, Ram S" uniqKey="Upadhyay R" first="Ram S." last="Upadhyay">Ram S. Upadhyay</name>
<name sortKey="Zehra, Andleeb" sort="Zehra, Andleeb" uniqKey="Zehra A" first="Andleeb" last="Zehra">Andleeb Zehra</name>
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<country name="Irlande (pays)"><noRegion><name sortKey="Gupta, Vijai K" sort="Gupta, Vijai K" uniqKey="Gupta V" first="Vijai K." last="Gupta">Vijai K. Gupta</name>
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