<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Leong JX</submitter><funding>Svenska Forskningsrådet Formas</funding><funding>Vetenskapsrådet</funding><funding>Deutsche Forschungsgemeinschaft</funding><funding>Division of Integrative Organismal Systems</funding><funding>Biotechnology and Biological Sciences Research Council</funding><funding>HORIZON EUROPE Marie Sklodowska-Curie Actions</funding><pagination>e110352</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9251887</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>41(13)</volume><pubmed_abstract>Beyond its role in cellular homeostasis, autophagy plays anti- and promicrobial roles in host-microbe interactions, both in animals and plants. One prominent role of antimicrobial autophagy is to degrade intracellular pathogens or microbial molecules, in a process termed xenophagy. Consequently, microbes evolved mechanisms to hijack or modulate autophagy to escape elimination. Although well-described in animals, the extent to which xenophagy contributes to plant-bacteria interactions remains unknown. Here, we provide evidence that Xanthomonas campestris pv. vesicatoria (Xcv) suppresses host autophagy by utilizing type-III effector XopL. XopL interacts with and degrades the autophagy component SH3P2 via its E3 ligase activity to promote infection. Intriguingly, XopL is targeted for degradation by defense-related selective autophagy mediated by NBR1/Joka2, revealing a complex antagonistic interplay between XopL and the host autophagy machinery. Our results implicate plant antimicrobial autophagy in the depletion of a bacterial virulence factor and unravel an unprecedented pathogen strategy to counteract defense-related autophagy in plant-bacteria interactions.</pubmed_abstract><journal>The EMBO journal</journal><pubmed_title>A bacterial effector counteracts host autophagy by promoting degradation of an autophagy component.</pubmed_title><pmcid>PMC9251887</pmcid><funding_grant_id>2016‐01044</funding_grant_id><funding_grant_id>SFB1101</funding_grant_id><funding_grant_id>BB/T006102/1</funding_grant_id><funding_grant_id>GZ</funding_grant_id><funding_grant_id>BO1961/5‐2</funding_grant_id><funding_grant_id>799433</funding_grant_id><funding_grant_id>2016‐04562</funding_grant_id><funding_grant_id>2026368</funding_grant_id><funding_grant_id>UE188/2‐1</funding_grant_id><funding_grant_id>2020‐05327</funding_grant_id><funding_grant_id>2017‐01596</funding_grant_id><pubmed_authors>Bornke F</pubmed_authors><pubmed_authors>Raffeiner M</pubmed_authors><pubmed_authors>Guzman AR</pubmed_authors><pubmed_authors>Franz-Wachtel M</pubmed_authors><pubmed_authors>Leong JX</pubmed_authors><pubmed_authors>Bozkurt TO</pubmed_authors><pubmed_authors>Ustun S</pubmed_authors><pubmed_authors>Pandey P</pubmed_authors><pubmed_authors>Spinti D</pubmed_authors><pubmed_authors>Hofius D</pubmed_authors><pubmed_authors>Hafren A</pubmed_authors><pubmed_authors>Kim JG</pubmed_authors><pubmed_authors>Langin G</pubmed_authors><pubmed_authors>Mudgett MB</pubmed_authors><pubmed_authors>Minina AE</pubmed_authors><pubmed_authors>Macek B</pubmed_authors></additional><is_claimable>false</is_claimable><name>A bacterial effector counteracts host autophagy by promoting degradation of an autophagy component.</name><description>Beyond its role in cellular homeostasis, autophagy plays anti- and promicrobial roles in host-microbe interactions, both in animals and plants. One prominent role of antimicrobial autophagy is to degrade intracellular pathogens or microbial molecules, in a process termed xenophagy. Consequently, microbes evolved mechanisms to hijack or modulate autophagy to escape elimination. Although well-described in animals, the extent to which xenophagy contributes to plant-bacteria interactions remains unknown. Here, we provide evidence that Xanthomonas campestris pv. vesicatoria (Xcv) suppresses host autophagy by utilizing type-III effector XopL. XopL interacts with and degrades the autophagy component SH3P2 via its E3 ligase activity to promote infection. Intriguingly, XopL is targeted for degradation by defense-related selective autophagy mediated by NBR1/Joka2, revealing a complex antagonistic interplay between XopL and the host autophagy machinery. Our results implicate plant antimicrobial autophagy in the depletion of a bacterial virulence factor and unravel an unprecedented pathogen strategy to counteract defense-related autophagy in plant-bacteria interactions.</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Jul</publication><modification>2024-11-13T08:38:56.39Z</modification><creation>2022-07-19T22:49:09.081Z</creation></dates><accession>S-EPMC9251887</accession><cross_references><pubmed>35620914</pubmed><doi>10.15252/embj.2021110352</doi></cross_references></HashMap>