Back to Search Start Over

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

Authors :
Xavier Foissac
Christophe Garcion
Frédérique Razan
Laure Béven
Sandrine Eveillard
Delphine Desqué
Camille Jollard
Biologie du fruit et pathologie (BFP)
Université de Bordeaux (UB)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
Source :
International Journal of Molecular Sciences, Vol 21, Iss 1, p 150 (2019), International Journal of Molecular Sciences, International Journal of Molecular Sciences, MDPI, 2020, 21 (1), pp.150. ⟨10.3390/ijms21010150⟩, International Journal of Molecular Sciences 1 (21), 150. (2020), Volume 21, Issue 1
Publication Year :
2020
Publisher :
MDPI, 2020.

Abstract

Flavescence dor&eacute<br />e (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 &ldquo<br />Candidatus Phytoplasma mali&rdquo<br />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.

Details

Language :
English
ISSN :
16616596 and 14220067
Database :
OpenAIRE
Journal :
International Journal of Molecular Sciences, Vol 21, Iss 1, p 150 (2019), International Journal of Molecular Sciences, International Journal of Molecular Sciences, MDPI, 2020, 21 (1), pp.150. ⟨10.3390/ijms21010150⟩, International Journal of Molecular Sciences 1 (21), 150. (2020), Volume 21, Issue 1
Accession number :
edsair.doi.dedup.....74f0b4a53d136c721c89bd176429d055
Full Text :
https://doi.org/10.3390/ijms21010150⟩