Dataset Information

Proximity labeling of OsPUX8B.2 interacting proteins with TurboID

ABSTRACT: Ubiquitin regulatory X (UBX) domain-containing proteins are one of the major subgroups of cofactors of the AAA+ ATPase CDC48/p97 and function in protein quality control involved in diverse cellular processes. However, little is known whether and how the UBX-containing proteins participate in host-microbe interaction. Here, we report a host nucleus-localized effector from Magnaporthe oryzae, MoNLE1, functions as a virulence factor and suppresses rice immunity by specially interferes with a rice UBX-containing (PUX) protein OsPUX8B.2. To reveal the working mechanism of OsPUX8B.2, we performed TurboID-based proximity labeling experiments to probe OsPUX8B.2 interaction proteins. The result showed that OsPUX8B.2 associates with a set of proteins involved in RNA processing and modification, protein folding and heat/light responses. We verified that a SGS domain-containing protein OsBHT, which negatively regulates rice defense against blast pathogen, is targeted by OsPUX8B.2-OsCDC48-6 for subsequent degradation.

ORGANISM(S): Oryza Sativa

SUBMITTER: Wende Liu

PROVIDER: PXD040074 | iProX | Tue May 23 00:00:00 BST 2023

REPOSITORIES: iProX

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Publications

A fungal core effector exploits the OsPUX8B.2-OsCDC48-6 module to suppress plant immunity.

Shi Xuetao X Xie Xin X Guo Yuanwen Y Zhang Junqi J Gong Ziwen Z Zhang Kai K Mei Jie J Xia Xinyao X Xia Haoxue H Ning Na N Xiao Yutao Y Yang Qing Q Wang Guo-Liang GL Liu Wende W

Nature communications 20240322 1

Proteins containing a ubiquitin regulatory X (UBX) domain are cofactors of Cell Division Cycle 48 (CDC48) and function in protein quality control. However, whether and how UBX-containing proteins participate in host-microbe interactions remain unclear. Here we show that MoNLE1, an effector from the fungal pathogen Magnaporthe oryzae, is a core virulence factor that suppresses rice immunity by specifically interfering with OsPUX8B.2. The UBX domain of OsPUX8B.2 is required for its binding to OsAT ...[more]

PMID: 38519521

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Project description:Oral health is associated with a symbiotic microbial community and host-microbe homeostasis is maintained by the controlled immune response. Various factors can disrupt this homeostasis. Dysbiosis, which is characterized by increased immune response and a shift in the microbiome, contributes the pathogenesis of peri-implantitis. Peri-implant mucosa and commensal bacteria play important roles in the maintenance of host-microbe homeostasis, but little is known about how they interact. We have therefore investigated the early host-microbe interaction between a commensal multispecies biofilm (Streptococcus oralis, Actinomyces naeslundii, Veillonella dispar, Porphyromonas gingivalis) and peri-implant mucosa at 24 and 48 h. Our in vitro peri-implant mucosa-biofilm model contained organotypic oral mucosa, implant material and biofilm. After 24 h, the biofilm induced a modest innate immune response in the peri-implant mucosa by the upregulation of 5 genes related to immune and inflammatory response and the increased secretion of IL-6 and CCL20. This controlled immune response protected tissue integrity and the peri-implant mucosa remained intact. The secreted antibacterial proteins human β-Defensins-1, -2, and CCL20 controlled the overgrowth of the biofilm by reducing its volume - without affecting the live/dead ratio or bacterial distribution. Thus, host-microbe homeostasis was established within the first 24 h. In contrast, host-microbe homeostasis was disrupted after 48 h. The mucosa was damaged and detached from the implant, due to the induced downregulation of cell adhesion related genes. The immune response was enhanced by upregulation of additional genes related to the immune and inflammatory response and increased secretion of IL-1β, TNF-α, and CCL20. Moreover, bacterial distribution was altered, with an increased proportion of V. dispar. The disrupted host-microbe homeostasis could lead to incipient dysbiosis. This deeper understanding of the early host-microbe interaction at the peri-implant site may provide the basis for new strategies to improve the prevention and therapy of peri-implant diseases.

Dataset Information

Proximity labeling of OsPUX8B.2 interacting proteins with TurboID

Publications

A fungal core effector exploits the OsPUX8B.2-OsCDC48-6 module to suppress plant immunity.

Similar Datasets

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