Characterization of the membrane-associated HaRxL17 Hpa effector candidate.
We examined changes to subcellular architecture during the compatible interaction between the biotroph pathogen Hyaloperonospora arabidopsidis (Hpa) and its host Arabidopsis. Live-cell imaging highlighted rearrangements in plant cell membranes upon infection. In particular, the tonoplast appeared close to the extrahaustorial membrane surrounding the haustorium. We investigated the subcellular localization patterns of Hpa RxLR effector candidates (HaRxLs) in planta. This subcellular localization screening led to the identification of an extrahaustorial membrane-localized effector, HaRxL17 that when stably expressed in Arabidopsis increased plant susceptibility to Hpa during compatible and incompatible interactions. Here, we report that the N-terminal part of HaRxL17 is sufficient to target the plant cell membranes. We showed that both C- or N-terminal fluorescent-tagged HaRxL17 localizes around Hpa haustoria, in early and in late stages of infection. As with Hpa infection, GFP-HaRxL17 also localizes around haustoria during infection with Albugo laibachii. Thus, HaRxL17 that increases plant susceptibility to Hpa during both compatible and incompatible interactions, localizes around oomycete haustoria when stably expressed in Arabidopsis.
The Sainsbury Laboratory, John Innes Centre, Norwich Research Park, Norwich, UK.
Marie-Cécile
MC
Caillaud
Sophie J M
SJ
Piquerez
Jonathan D G
JD
Jones
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000382:microbiology*; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D009868:Oomycetes / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D013347:Subcellular Fractions / Q000378:metabolism
D029681:Arabidopsis Proteins; D008565:Membrane Proteins