RT Conference Proceedings
T1 Role of chemotaxis cluster II in pathogenic bacteria of woody and herbaceous plants.
A1 Lavado-Benito, Carla
A1 Rodríguez-Moreno, Luis Gabriel
A1 Santamaría-Hernando, Saray
A1 López-Solanilla, Emilia
A1 Ramos-Rodríguez, Cayo Juan
K1 Bacterias fitopatógenas
K1 Plantas - Enfermedades bacterianas
AB Chemoreceptors are essential proteins able to detect environmental changes forbacterial adaptation to the environment. The genes encoding these proteins arefound individually in the genome or forming clusters with other genes related tochemotaxis. In plant-pathogenic bacteria, about 82 thousand chemosensorysequences have been described (1). In the Pseudomonas syringae complex, oneof the most important groups of plant-pathogenic bacteria, four chemotaxisrelatedclusters have been described. However, one of these clusters, namedcluster II, is absent in some bacteria of this complex infecting woody hosts of theApocinaceae family. Examples of the absence of this cluster are strains ofPseudomonas savastanoi pv. mandevillae (Psm) and some strains of P.savastanoi pv. nerii (Psn), isolated from dipladenia (Mandevilla spp.) andoleander (Nerium oleander), respectively. Therefore, the aim of this work focuseson the functional characterization of cluster II, not only in bacteria isolated fromwoody hosts, but also in strains infecting herbaceous plants.First, we constructed knockout mutants of most genes encoded in cluster II, i.e.cheA, cheB, cheD, cheY and two genes coding for chemoreceptors in a woodyplant pathogenic strain, both in Psn23 strain and in P. syringae pv. tomato (Pto)DC3000. Motility and virulence assays performed in oleander, dipladenia andtomato plants revealed that cluster II is involved in both phenotypes. In addition,bioinformatic analysis of the ligand-binding domain (LBD) (1) of the twochemoreceptors encoded in cluster II showed that only one of them has an LBDdomain. To characterise this chemoreceptor in strain Psn23, capillaritychemotaxis assays are being performed, and its LBD domain has been purified.The purified domain will be used in protein-ligand interaction assays against acollection of plant-derived compounds.
PB International Society for plant pathology
YR 2023
FD 2023
LK https://hdl.handle.net/10630/27899
UL https://hdl.handle.net/10630/27899
LA eng
NO Universidad de Málaga. Campus de Excelencia Internacional Andalucía Tech.
DS RIUMA. Repositorio Institucional de la Universidad de Málaga
RD 20 ene 2026