Flavescence Dorée Phytoplasma Has Multiple <i>ftsH</i> Genes that Are Differentially Expressed in Plants and Insects

• Main Authors: Camille Jollard, Xavier Foissac, Delphine Desqué, Frédérique Razan, Christophe Garcion, Laure Beven, Sandrine Eveillard
• Format: Article
• Language: English
• Published: MDPI AG 2019-12-01
• Series: International Journal of Molecular Sciences
• Subjects: phytoplasmas; membrane proteases; protein metabolism; virulence
• Online Access: https://www.mdpi.com/1422-0067/21/1/150

Flavescence dor&#233;e (FD) is a severe epidemic disease of grapevines caused by FD phytoplasma (FDP) transmitted by the leafhopper vector <i>Scaphoideus titanus</i>. 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 &#8220;<i>Candidatus</i> Phytoplasma mali&#8221; 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 <i>ftsH</i> genes have been identified in the FDP genome. In addition to <i>ftsH</i>6, 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 <i>ftsH</i>. 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.