{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T20:05:37Z","timestamp":1784837137943,"version":"3.55.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1014382","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T00:00:00Z","timestamp":1784764800000}}],"reference-count":96,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2026,7,13]],"date-time":"2026-07-13T00:00:00Z","timestamp":1783900800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Phytopathogenic fungi secrete effector proteins to promote virulence. The MAX (\n                    <jats:italic>Magnaporthe<\/jats:italic>\n                    Avrs and ToxB-like) effectors form a structurally conserved family despite significant sequence diversity. AVR-Pia, a MAX effector from the rice blast fungus\n                    <jats:italic>Magnaporthe oryzae,<\/jats:italic>\n                    is recognised by the model rice nucleotide-binding leucine-rich repeat (NLR) receptor pair OsRGA4\/OsRGA5 via direct binding to a heavy metal-associated (HMA) integrated domain (ID) in OsRGA5. While the structural basis of AVR-Pia recognition is well defined, the role of this effector in promoting virulence has remained elusive. Here, we reveal that AVR-Pia specifically interacts with four previously uncharacterised rice HMA domain-containing proteins, three HMA Plant Proteins (OsHPP09, OsHPP10 and OsHPP11), and one HMA Isoprenylated Plant Protein (OsHIPP21). AVR-Pia binds these proteins in vitro and in planta, engaging their HMA domains with differential affinities. Notably, AVR-Pia binds OsHPP09-HMA with considerably higher affinity than the HMA-ID of OsRGA5. By solving the crystal structure of the AVR-Pia\/OsHPP09-HMA complex, we identified additional molecular contacts at the interface which underpin high affinity binding. Importantly, the H(I)PPs identified as AVR-Pia interactors are distinct from those bound by the MAX effectors AVR-Pik and Pwl2, underscoring target specialisation within the MAX effector family. Further, structural analyses of the AVR-Pia\/OsHPP09-HMA complex revealed a markedly different interface compared to other MAX effector\/H(I)PP complexes. Finally, structure-guided mutagenesis of OsHPP09 identified a single residue that is critical for AVR-Pia binding. This work provides structural insight into how distinct MAX effectors exploit HMA domain-containing proteins and offers a foundation towards targeted modification of HMA domains to disrupt effector binding and enhance cereal resistance to blast disease.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1014382","type":"journal-article","created":{"date-parts":[[2026,7,13]],"date-time":"2026-07-13T17:44:06Z","timestamp":1783964646000},"page":"e1014382","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["Two folds, many faces: The Magnaporthe oryzae MAX effector AVR-Pia targets novel rice HMA domain-containing proteins"],"prefix":"10.1371","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8229-2718","authenticated-orcid":true,"given":"Josephine H. R.","family":"Maidment","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2258-3166","authenticated-orcid":true,"given":"Svenja C.","family":"Saile","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0007-0082-6098","authenticated-orcid":true,"given":"Aur\u00e9lien","family":"Bocquet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-5048-3619","authenticated-orcid":true,"given":"C\u00e9line","family":"Thivolle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-4568-3543","authenticated-orcid":true,"given":"L\u00e9o","family":"Bourcet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0007-5159-7109","authenticated-orcid":true,"given":"Lisa-Fatimatou","family":"Planel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1320-8663","authenticated-orcid":true,"given":"Muriel","family":"Gelin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3752-1788","authenticated-orcid":true,"given":"Thomas","family":"Kroj","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9702-4612","authenticated-orcid":true,"given":"Andr\u00e9","family":"Padilla","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5037-2115","authenticated-orcid":true,"given":"Karine","family":"de Guillen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8558-0371","authenticated-orcid":true,"given":"Stella","family":"Cesari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2026,7,13]]},"reference":[{"issue":"4","key":"ppat.1014382.ref001","doi-asserted-by":"crossref","DOI":"10.1111\/mpp.13449","article-title":"Pyricularia oryzae: Lab star and field scourge","volume":"25","author":"M Baudin","year":"2024","journal-title":"Mol Plant Pathol"},{"issue":"3","key":"ppat.1014382.ref002","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1038\/s41559-018-0793-y","article-title":"The global burden of pathogens and pests on major food crops","volume":"3","author":"S Savary","year":"2019","journal-title":"Nat Ecol Evol"},{"issue":"4","key":"ppat.1014382.ref003","doi-asserted-by":"crossref","first-page":"1460","DOI":"10.1111\/nph.70075","article-title":"Structure-guided insights into the biology of fungal effectors","volume":"246","author":"M Le Naour-Vernet","year":"2025","journal-title":"New Phytol"},{"issue":"10","key":"ppat.1014382.ref004","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005228","article-title":"Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi","volume":"11","author":"K de Guillen","year":"2015","journal-title":"PLoS Pathog"},{"issue":"16","key":"ppat.1014382.ref005","doi-asserted-by":"crossref","first-page":"6068","DOI":"10.3390\/molecules28166068","article-title":"Does a Similar 3D Structure Mean a Similar Folding Pathway? 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