Intrinsically Disordered Kiwellin Protein-Like Effectors Target Plant Chloroplasts and are Extensively Present in Rust Fungi

Jaswal, Rajdeep; Rajarammohan, Sivasubramanian; Dubey, Himanshu; Kiran, Kanti; Rawal, Hukam C.; Sonah, Humira; Deshmukh, Rupesh; Sharma, Tilak Raj

doi:10.1007/s12033-023-00717-y

Cited by 2 publications

(3 citation statements)

References 61 publications

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“…In many cases, terminal extensions appeared as unstructured regions that could not be modeled with high confidence by AF2. Long intrinsic disordered regions (IDRs) of more than 30 a.a. [ 26 – 28 ] may have diverse function in bacterial [ 29 , 30 ] and fungal effectors [ 31 , 32 ] and we therefore searched for IDR signatures in MAX effector sequences using ESpritz prediction software [ 33 ]. Long IDRs were predicted for ten MAX effectors and were unstructured in six AF_MAX models: in MAX15 (118 a.a.), MAX27 (36 a.a.) and MAX43 (43 a.a) as N-ter extensions, and in MAX28 (42 a.a.), MAX53 (38 a.a.) and MAX78 (43 a.a.) as C-ter extensions.…”

Section: Resultsmentioning

confidence: 99%

The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited

Lahfa,

Barthe,

de Guillen

et al. 2024

PLoS Pathog

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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.

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Section: Resultsmentioning

confidence: 99%

The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited

Lahfa,

Barthe,

de Guillen

et al. 2024

PLoS Pathog

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“…There are also many examples where terminal extensions appear as unstructured regions that could not be modeled with high confidence by AlphaFold2. Long intrinsic disordered regions (IDRs) of more than 30 a.a. [21–23] may have diverse function in bacterial [24,25] and fungal effectors [26,27] and we had therefore searched for IDR signatures in MAX effector sequences using ESpritz prediction software [28]. Long IDRs were predicted for only a few MAX effectors and their presence was cross-validated for six AF_MAX models: in MAX15 (118 a.a.), MAX27 (36 a.a.) and MAX43 (43 a.a) as N- ter extensions, and in MAX28 (42 a.a.), MAX53 (49 a.a.) and MAX78 (43 a.a.) as C- ter extensions.…”

Section: Resultsmentioning

confidence: 99%

“…In many cases, terminal extensions appeared as unstructured regions that could not be modeled with high confidence by AF2. Long intrinsic disordered regions (IDRs) of more than 30 a.a. [24-26] may have diverse function in bacterial [27,28] and fungal effectors [29,30] and we therefore searched for IDR signatures in MAX effector sequences using ESpritz prediction software [31]. Long IDRs were predicted for ten MAX effectors and were unstructured in six AF_MAX models: in MAX15 (118 a.a.), MAX27 (…”

Section: N-and C-terminal Extensionsmentioning

confidence: 99%

The structural landscape and diversity ofPyricularia oryzaeMAX effectors revisited

Lahfa,

Barthe,

De Guillen

et al. 2023

Preprint

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Plant pathogenic fungi secrete a wide variety of small proteins, named effectors.MagnaportheAVRs and ToxB-like (MAX) effectors constitute a superfamily of secreted proteins widely distributed inPyricularia (syn. Magnaporthe) oryzae, a devastating fungus responsible for blast disease in cereals such as rice. In spite of high evolutionary sequence divergence, MAX effectors share a common fold characterized by a ß-sandwich core often stabilized by a conserved disulfide bond. In this study, we investigated the structural landscape and diversity within this effector family based on a previous phylogenetic analysis ofP. oryzaeprotein sequences that identified 94 ortholog groups (OG) of putative MAX effectors. Combining protein structure modeling approaches and experimental structure determination, we validated the prediction of the conserved MAX core domain for 77 OG clusters. Four novel MAX effector structures determined by NMR were in remarkably good agreement with AlphaFold2 (AF) predictions. Based on the comparison of the AF-generated 3D models we propose an updated classification of the MAX effectors superfamily in 20 structural groups that highlight variation observed in the canonical MAX fold, disulfide bond patterns and decorating secondary structures in N- and C-terminal extensions. About one-third of the MAX family members remain single, showing no obvious structural relationship with other MAX effectors. Analysis of the surface properties of the AF MAX models also highlights the very high variability remaining within the MAX family when examined at the structural level, probably reflecting the wide diversity of their virulence functions and host targets.Author summaryMAX effectors are a family of virulence proteins from the plant pathogenic fungusPyricularia (syn. Magnaporthe) oryzaethat share a similar 3D structure despite very low amino-acid sequence identity. Characterizing the function and evolution of these proteins requires a detailed understanding of their structural diversity. We used a combination of experimental structure determination and structural modeling to characterize in detail the MAX effector repertoire ofP. oryzae. A prediction pipeline based on similarity searches and structural modeling using the AlphaFold2 (AF) software were used to predict MAX effectors in a collection of 120P. oryzaegenomes. We then compared AF models with experimentally validated NMR structures. The resulting models and experimental structures revealed that the preserved MAX core coexists with extensive structural variability in terms of structured N- or C-terminal extensions. For each of the AF models, we also analyzed the surfaces of the canonical fold that may be involved in protein-protein interactions. This work constitutes a major step in mapping the functional network of MAX effectors through their structure by identifying possible recognition sites that may help focusing studies of their putative targets in infected plant hosts.

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Intrinsically Disordered Kiwellin Protein-Like Effectors Target Plant Chloroplasts and are Extensively Present in Rust Fungi

Cited by 2 publications

References 61 publications

The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited

The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited

The structural landscape and diversity ofPyricularia oryzaeMAX effectors revisited

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