Sulfated RaxX, which represents an unclassified group of ribosomally synthesized post-translationally modified peptides, binds a host immune receptor
| Autor: | Rory N Pruitt, Christopher J. Petzold, Yan Chen, Dee Dee Luu, Kanya C. Long, Anna Joe, Chen Ljg, Stewart, Youssef Belkhadir, Clifford Adamchak, Katarzyna Parys, Ofir Bahar, Pamela C. Ronald |
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| Rok vydání: | 2018 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Immunogen Protease biology 030306 microbiology Chemistry medicine.medical_treatment Peptide Immune receptor biology.organism_classification 03 medical and health sciences chemistry.chemical_compound Xanthomonas oryzae Biochemistry Biosynthesis medicine Secretion Receptor 030304 developmental biology |
| Popis: | The rice immune receptor XA21 is activated by the sulfated microbial peptide RaxX (required foractivation ofXA21-mediated immunityX) produced byXanthomonas oryzaepv.oryzae(Xoo). Mutational studies and targeted proteomics revealed that RaxX is processed and secreted by the protease/transporter RaxB, whose function can be partially fulfilled by a noncognatepeptidase-containing transporterB(PctB). RaxX is cleaved at a Gly-Gly motif, yielding a mature peptide that retains the necessary elements for RaxX function as an immunogen and host peptide hormone mimic. These results indicate that RaxX is a founding member of a previously unclassified and understudied group of tyrosine sulfated RiPPs (ribosomally synthesized,post-translationally modifiedpeptides). We further demonstrate that sulfated RaxX directly binds XA21 with high affinity. This work reveals a complete, previously uncharacterized biological process: bacterial RiPP biosynthesis, secretion, binding to a eukaryotic receptor and triggering of a robust host immune response. |
| Databáze: | OpenAIRE |
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