The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited.
Magnaporthe AVRs and ToxB-like (MAX) effectors constitute a family of secreted virulence proteins in the fungus Pyricularia oryzae (syn. Magnaporthe oryzae), which causes blast disease on numerous cereals and grasses. In spite of high sequence divergence, MAX effectors share a common fold characteri...
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Public Library of Science (PLoS)
2024-05-01
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| Series: | PLoS Pathogens |
| Online Access: | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1012176&type=printable |
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| author | Mounia Lahfa Philippe Barthe Karine de Guillen Stella Cesari Mouna Raji Thomas Kroj Marie Le Naour-Vernet François Hoh Pierre Gladieux Christian Roumestand Jérôme Gracy Nathalie Declerck André Padilla |
| author_facet | Mounia Lahfa Philippe Barthe Karine de Guillen Stella Cesari Mouna Raji Thomas Kroj Marie Le Naour-Vernet François Hoh Pierre Gladieux Christian Roumestand Jérôme Gracy Nathalie Declerck André Padilla |
| author_sort | Mounia Lahfa |
| collection | DOAJ |
| description | Magnaporthe AVRs and ToxB-like (MAX) effectors constitute a family of secreted virulence proteins in the fungus Pyricularia oryzae (syn. Magnaporthe oryzae), which causes blast disease on numerous cereals and grasses. In spite of high sequence divergence, MAX effectors share a common fold characterized by a ß-sandwich core stabilized by a conserved disulfide bond. In this study, we investigated the structural landscape and diversity within the MAX effector repertoire of P. oryzae. Combining experimental protein structure determination and in silico structure modeling we validated the presence of the conserved MAX effector core domain in 77 out of 94 groups of orthologs (OG) identified in a previous population genomic study. Four novel MAX effector structures determined by NMR were in remarkably good agreement with AlphaFold2 (AF2) predictions. Based on the comparison of the AF2-generated 3D models we propose a classification of the MAX effectors superfamily in 20 structural groups that vary in the canonical MAX fold, disulfide bond patterns, and additional secondary structures in N- and C-terminal extensions. About one-third of the MAX family members remain singletons, without strong structural relationship to other MAX effectors. Analysis of the surface properties of the AF2 MAX models also highlights the high variability within the MAX family at the structural level, potentially reflecting the wide diversity of their virulence functions and host targets. |
| format | Article |
| id | doaj-art-05ba20d0e9b1499aaf7604f2e1ef2251 |
| institution | Kabale University |
| issn | 1553-7366 1553-7374 |
| language | English |
| publishDate | 2024-05-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj-art-05ba20d0e9b1499aaf7604f2e1ef22512025-01-16T05:30:58ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742024-05-01205e101217610.1371/journal.ppat.1012176The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited.Mounia LahfaPhilippe BartheKarine de GuillenStella CesariMouna RajiThomas KrojMarie Le Naour-VernetFrançois HohPierre GladieuxChristian RoumestandJérôme GracyNathalie DeclerckAndré PadillaMagnaporthe AVRs and ToxB-like (MAX) effectors constitute a family of secreted virulence proteins in the fungus Pyricularia oryzae (syn. Magnaporthe oryzae), which causes blast disease on numerous cereals and grasses. In spite of high sequence divergence, MAX effectors share a common fold characterized by a ß-sandwich core stabilized by a conserved disulfide bond. In this study, we investigated the structural landscape and diversity within the MAX effector repertoire of P. oryzae. Combining experimental protein structure determination and in silico structure modeling we validated the presence of the conserved MAX effector core domain in 77 out of 94 groups of orthologs (OG) identified in a previous population genomic study. Four novel MAX effector structures determined by NMR were in remarkably good agreement with AlphaFold2 (AF2) predictions. Based on the comparison of the AF2-generated 3D models we propose a classification of the MAX effectors superfamily in 20 structural groups that vary in the canonical MAX fold, disulfide bond patterns, and additional secondary structures in N- and C-terminal extensions. About one-third of the MAX family members remain singletons, without strong structural relationship to other MAX effectors. Analysis of the surface properties of the AF2 MAX models also highlights the high variability within the MAX family at the structural level, potentially reflecting the wide diversity of their virulence functions and host targets.https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1012176&type=printable |
| spellingShingle | Mounia Lahfa Philippe Barthe Karine de Guillen Stella Cesari Mouna Raji Thomas Kroj Marie Le Naour-Vernet François Hoh Pierre Gladieux Christian Roumestand Jérôme Gracy Nathalie Declerck André Padilla The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. PLoS Pathogens |
| title | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. |
| title_full | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. |
| title_fullStr | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. |
| title_full_unstemmed | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. |
| title_short | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. |
| title_sort | structural landscape and diversity of pyricularia oryzae max effectors revisited |
| url | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1012176&type=printable |
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