Understanding enemy’s weapons to an effective prevention: common virulence effects across microbial phytopathogens kingdoms

Kotsaridis, Konstantinos; Tsakiri, Dimitra; Sarris, Panagiotis F.

doi:10.1080/1040841x.2022.2083939

Cited by 7 publications

(9 citation statements)

References 132 publications

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“…1D ). RipE1 belongs to the HopX1/AvrPphE effector family, the members of which share a conserved N-terminal domain and a catalytic triad with predicted cysteine protease activity (54, 55, 60). RipE1 produced by the R. solanacearum RS1000 strain has been shown to possess this enzymatic activity and it seemingly depends on it to cleave JAZ repressors (49).…”

Section: Resultsmentioning

confidence: 99%

The core effector RipE1 ofRalstonia solanacearuminteracts with and cleaves Exo70B1 and is recognized by the Ptr1 immune receptor

Tsakiri

Kotsaridis

Michalopoulou

et al. 2022

Preprint

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Ralstonia solanacearum depends on numerous virulence factors, also known as effectors, to promote disease in a wide range of economically important host-plants. Although some of these effectors have been characterized, none has been shown to target the host secretion machinery so far. Here, a screening was performed, using an extended library of NLR plant immune receptors integrated domains (IDs), to identify new effector targets. The results uncovered that the core effector RipE1, of the R. solanacearum species complex, among other targets, associates with Arabidopsis exocyst component Exo70B1. RipE1, in accordance with its predicted cysteine protease activity, cleaves Exo70B1 in vitro between its sequence and is able to promote Exo70B1 degradation in planta. RipE1 enzymatic activity additionally results in the activation of TN2-dependent cell death. TN2 is an atypical NLR that has been proposed to guard Exo70B1. Despite the fact that RipE1 has been previously reported to activate defense responses in model plant species, we present here a Nicotiana species, in which RipE1 expression does not activate cell death. Overall, this study uncovers a new RipE1 host target, while providing evidence and novel tools to advance in-depth studies of RipE1 and homologues effectors.

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Section: Resultsmentioning

confidence: 99%

The core effector RipE1 ofRalstonia solanacearuminteracts with and cleaves Exo70B1 and is recognized by the Ptr1 immune receptor

Tsakiri

Kotsaridis

Michalopoulou

et al. 2022

Preprint

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“…Being the components of an essential cellular mechanism, exocyst subunits are often targeted by pathogens that manipulate host cell physiology (Michalopoulou et al., 2022; Tsakiri et al., 2022; Wang et al., 2019). Successful plant pathogens use an arsenal of protein effectors, which display a variety of functions (Kotsaridis et al., 2022). These virulence molecules are secreted in host tissues or injected inside the host cells and target diverse processes, in order to bypass host defense mechanisms (Büttner & Bonas, 2003; Kotsaridis et al., 2022; Sertedakis et al., 2022).…”

Section: Discussionmentioning

confidence: 99%

“…Effector structural studies grant valuable insight into effector biology, especially in the context of creating novel strategies against pathogens (Kotsaridis et al., 2022; LeBlanc et al., 2021; Mak & Thurston, 2021). Although the classical techniques for protein structure identification can be difficult and, in some cases impossible, the rapid development of artificial intelligence (AI) software, like AlphaFold, can provide very accurate protein structure prediction (Tunyasuvunakool, 2022).…”

Section: Introductionmentioning

confidence: 99%

The functional and structural characterization of Xanthomonas campestris pv. campestris core effector XopP revealed a new kinase activity

et al. 2023

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SUMMARYExo70B1 is a protein subunit of the exocyst complex with a crucial role in a variety of cell mechanisms, including immune responses against pathogens. The calcium‐dependent kinase 5 (CPK5) of Arabidopsis thaliana (hereafter Arabidopsis), phosphorylates AtExo70B1 upon functional disruption. We previously reported that, the Xanthomonas campestris pv. campestris effector XopP compromises AtExo70B1, while bypassing the host's hypersensitive response, in a way that is still unclear. Herein we designed an experimental approach, which includes biophysical, biochemical, and molecular assays and is based on structural and functional predictions, utilizing AplhaFold and DALI online servers, respectively, in order to characterize the in vivo XccXopP function. The interaction between AtExo70B1 and XccXopP was found very stable in high temperatures, while AtExo70B1 appeared to be phosphorylated at XccXopP‐expressing transgenic Arabidopsis. XccXopP revealed similarities with known mammalian kinases and phosphorylated AtExo70B1 at Ser107, Ser111, Ser248, Thr309, and Thr364. Moreover, XccXopP protected AtExo70B1 from AtCPK5 phosphorylation. Together these findings show that XccXopP is an effector, which not only functions as a novel serine/threonine kinase upon its host target AtExo70B1 but also protects the latter from the innate AtCPK5 phosphorylation, in order to bypass the host's immune responses. Data are available via ProteomeXchange with the identifier PXD041405.

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“…Many pathogens use protein effectors, which reveal a variety of functions. These effectors are injected into the host cells helping pathogens to bypass host defense mechanisms (Büttner and Bonas, 2003; Kotsaridis, Tsakiri and Sarris, 2022; Sertedakis et al, 2022).…”

Section: Discussionmentioning

confidence: 99%

“…It is well established that effectors’ structural biology studies can be a revealing factor, changing the concept of creating novel strategies against pathogens (LeBlanc et al ., 2021; Mak and Thurston, 2021; Kotsaridis, Tsakiri and Sarris, 2022). Although the classical techniques for protein structure identification can be difficult and, in some cases impossible, the rapid development of artificial intelligence software, like Alphafold, can be very accurate for protein structures’ prediction (Tunyasuvunakool, 2022).…”

Section: Introductionmentioning

confidence: 99%

The functional and structural characterization ofXanthomonas campestrispv.campestriscore effector XopP revealed a new kinase activity

Kotsaridis

Michalopoulou

Tsakiri

et al. 2022

Preprint

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The exocyst complex subunit protein Exo70B1 plays a crucial role in a variety of cell mechanisms including immune responses against pathogens. The calcium dependent kinase 5 (CPK5) of Arapidopsis thaliana, phosphorylates AtExo70B1 upon functional disruption. We previously reported that, the Xanthomonas campestris pv. campestis effector XopP, compromises Exo70B1 and bypasses the host's hypersensitive response (HR), in a way that is still unclear. Herein we designed an experimental approach based on biophysical, biochemical and molecular assays, based on structural and functional predictions, as well as, utilizing Aplhafold and DALI online servers respectively, in order to characterize the in vivo XccXopP function. The interaction between AtExo70B1 and XccXopP is very stable in high temperatures, while the AtExo70B1 appeared to be phosphorylated at XccXopP expressing transgenic Arabidopsis. XccXopP reveals similarities with known mammalian kinases, and phosphorylates AtExo70B1 at Ser107, Ser111, Ser248, Thr309 and Thr364. Furthermore, XccXopP protects AtExo70B1 from AtCPK5 phosphorylation. Together these findings show that, XccXopP is an effector, which not only functions as a novel serine/threonine kinase upon its host's protein target AtExo70B1, but also protects the latter from the innate AtCPK5 phosphorylation, to bypass the host's immune responses.

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Understanding enemy’s weapons to an effective prevention: common virulence effects across microbial phytopathogens kingdoms

Cited by 7 publications

References 132 publications

The core effector RipE1 ofRalstonia solanacearuminteracts with and cleaves Exo70B1 and is recognized by the Ptr1 immune receptor

The core effector RipE1 ofRalstonia solanacearuminteracts with and cleaves Exo70B1 and is recognized by the Ptr1 immune receptor

The functional and structural characterization of Xanthomonas campestris pv. campestris core effector XopP revealed a new kinase activity

The functional and structural characterization ofXanthomonas campestrispv.campestriscore effector XopP revealed a new kinase activity

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