期刊
MOLECULAR PLANT-MICROBE INTERACTIONS
卷 34, 期 11, 页码 1267-1280出版社
AMER PHYTOPATHOLOGICAL SOC
DOI: 10.1094/MPMI-03-21-0071-R
关键词
computational structural genomics; effectors; fungal effectors; fungus-plant interactions; genomics; Magnaporthe oryzae; phytopathogen; structure
资金
- Berkeley Fellowship
- Gordon and Betty Moore Foundation [8802]
- Foundation for Food and Agriculture
- 2Blades [CA19-SS0000000046]
- Innovative Genomics Institute
Structural biology has the potential to illuminate the evolution of pathogen effectors and their commonalities, with recent breakthroughs in protein structure modeling enabling genome-wide computational approaches. In this study, structure prediction methods were applied to the secretome of the fungal pathogen Magnaporthe oryzae, revealing new members of structurally similar effectors and effector families. Additionally, the evolution of putative ADP-ribose transferases with predicted structures was investigated, suggesting new evolutionary trajectories for specialized protein binders.
Structural biology has the potential to illuminate the evolution of pathogen effectors and their commonalities that cannot be readily detected at the primary sequence level. Recent breakthroughs in protein structure modeling have demonstrated the feasibility to predict the protein folds without depending on homologous templates. These advances enabled a genome-wide computational structural biology approach to help understand proteins based on their predicted folds. In this study, we employed structure prediction methods on the secretome of the destructive fungal pathogen Magnaporthe oryzae. Out of 1,854 secreted proteins, we predicted the folds of 1,295 proteins (70%). We showed that template-free modeling by TrRosetta captured 514 folds missed by homology modeling, including many known effectors and virulence factors, and that TrRosetta generally produced higher quality models for secreted proteins. Along with sensitive homology search, we employed structure-based clustering, defining not only homologous groups with divergent members but also sequence-unrelated structurally analogous groups. We demonstrate that this approach can reveal new putative members of structurally similar MAX effectors and novel analogous effector families present in M. oryzae and possibly in other phytopathogens. We also investigated the evolution of expanded putative ADP-ribose transferases with predicted structures. We suggest that the loss of catalytic activities of the enzymes might have led them to new evolutionary trajectories to be specialized as protein binders. Collectively, we propose that computational structural genomics approaches can be an integral part of studying effector biology and provide valuable resources that were inaccessible before the advent of machine learning-based structure prediction.
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