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Flavescence Dorée Phytoplasma Has Multiple ftsH Genes that Are Differentially Expressed in Plants and Insects

hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorJOLLARD, Camille
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorFOISSAC, Xavier
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorDESQUE, Delphine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorRAZAN, Frédérique
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorGARCION, Christophe
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBÉVEN, Laure
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorEVEILLARD, Sandrine
dc.date.issued2020
dc.identifier.issn1661-6596
dc.description.abstractEnFlavescence dorée (FD) is a severe epidemic disease of grapevines caused by FD phytoplasma (FDP) transmitted by the leafhopper vector Scaphoideus titanus. The recent sequencing of the 647-kbp FDP genome highlighted an unusual number of genes encoding ATP-dependent zinc proteases FtsH, which have been linked to variations in the virulence of "Candidatus Phytoplasma mali" strains. The aims of the present study were to predict the FtsH repertoire of FDP, to predict the functional domains and topologies of the encoded proteins in the phytoplasma membrane and to measure the expression profiles in different hosts. Eight complete ftsH genes have been identified in the FDP genome. In addition to ftsH6, which appeared to be the original bacterial ortholog, the other seven gene copies were clustered on a common distinct phylogenetic branch, suggesting intra-genome duplication of ftsH. The expression of these proteins, quantified in plants and insect vectors in natural and experimental pathosystems, appeared to be modulated in a host-dependent manner. Two of the eight FtsH C-tails were predicted by Phobius software to be extracellular and, therefore, in direct contact with the host cellular content. As phytoplasmas cannot synthesize amino acids, our data raised questions regarding the involvement of FtsH in the adaptation to hosts via potentially enhanced recycling of phytoplasma cellular proteins and host protein degradation.
dc.language.isoen
dc.publisherMDPI
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.subjectprotein metabolism
dc.subject.enmembrane proteases
dc.subject.enphytoplasmas
dc.subject.envirulence
dc.title.enFlavescence Dorée Phytoplasma Has Multiple ftsH Genes that Are Differentially Expressed in Plants and Insects
dc.typeArticle de revue
dc.identifier.doi10.3390/ijms21010150
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie
bordeaux.journalInternational Journal of Molecular Sciences
bordeaux.page150
bordeaux.volume21
bordeaux.issue1
bordeaux.peerReviewedoui
hal.identifierhal-02627685
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02627685v1
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