Xanthomonas phaseoli pv. manihotis effector XopAO1 targets two key proteins to suppress defense in Cassava

dc.contributorBernal Giraldo, Adriana Jimena
dc.contributorGermain, Hugo
dc.contributorDíaz Tatis, Paula Alejandra
dc.contributorZimmermann, Barbara Hanna
dc.contributorLaboratorio de Interacciones Moleculares de Microorganismos Agrícolas (LIMMA)
dc.creatorCastillo, Darwin Alexander
dc.date.accessioned2023-01-18T13:49:38Z
dc.date.accessioned2023-09-07T00:48:13Z
dc.date.available2023-01-18T13:49:38Z
dc.date.available2023-09-07T00:48:13Z
dc.date.created2023-01-18T13:49:38Z
dc.date.issued2023-01-16
dc.identifierhttp://hdl.handle.net/1992/63947
dc.identifierinstname:Universidad de los Andes
dc.identifierreponame:Repositorio Institucional Séneca
dc.identifierrepourl:https://repositorio.uniandes.edu.co/
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8727804
dc.description.abstractThe Type Three Effector (TTE) protein AvrRpm1 of Pseudomonas syringae can contribute to pathogen virulence or induce an immune response in Arabidopsis, tomato, lettuce, and soybean by modifying their intracellular "guardee" plant protein, for example, AtRIN4. This triggers a resistance protein to halt pathogen proliferation. Other TTEs can directly interact with their host targets to bypass the plant immunity. Prior studies showed that Xanthomonas phaseoli pv. manihotis (Xpm), the causal agent of Cassava Bacterial Blight (CBB), uses the effector XopAO1 to suppress host Effector Triggered Immunity (ETI) and PAMP-triggered Immunity (PTI). Here, we used a yeast two-hybrid system and bioinformatic characterisation of two casava proteins and XopAO1 to investigate putative interactions involved in the development of CBB disease. Our results suggest that XopAO1 interacts with MeRIN4 and MeKinase full-length proteins. Also, we speculate that the XopAO1-MeRIN4 interaction is mediated by the ADP-ribosyl polymerase (PARP) domain in the N-terminal region of XopAO1, but domain-specific experimental interaction assays are needed. We also hypothesize that PARP-domain of XopAO1 might target either the C-NOI or the N-NOI domain of MeRIN4. Conversely, we determined that MeKinase harbours a protein kinase and NAF domains. At this point, we do not know the immunological consequences of XopAO1-MeKinase interaction, thus, further research will be required to elucidate this phenomenon.
dc.languageeng
dc.publisherUniversidad de los Andes
dc.publisherMaestría en Ciencias Biológicas
dc.publisherFacultad de Ciencias
dc.publisherDepartamento de Ciencias Biológicas
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dc.titleXanthomonas phaseoli pv. manihotis effector XopAO1 targets two key proteins to suppress defense in Cassava
dc.typeTrabajo de grado - Maestría


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