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RFPDR: a random forest approach for plant disease resistance protein prediction
BACKGROUND: Plant innate immunity relies on a broad repertoire of receptor proteins that can detect pathogens and trigger an effective defense response. Bioinformatic tools based on conserved domain and sequence similarity are within the most popular strategies for protein identification and charact...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
PeerJ Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9037127/ https://www.ncbi.nlm.nih.gov/pubmed/35480565 http://dx.doi.org/10.7717/peerj.11683 |
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author | Simón, Diego Borsani, Omar Filippi, Carla Valeria |
author_facet | Simón, Diego Borsani, Omar Filippi, Carla Valeria |
author_sort | Simón, Diego |
collection | PubMed |
description | BACKGROUND: Plant innate immunity relies on a broad repertoire of receptor proteins that can detect pathogens and trigger an effective defense response. Bioinformatic tools based on conserved domain and sequence similarity are within the most popular strategies for protein identification and characterization. However, the multi-domain nature, high sequence diversity and complex evolutionary history of disease resistance (DR) proteins make their prediction a real challenge. Here we present RFPDR, which pioneers the application of Random Forest (RF) for Plant DR protein prediction. METHODS: A recently published collection of experimentally validated DR proteins was used as a positive dataset, while 10x10 nested datasets, ranging from 400-4,000 non-DR proteins, were used as negative datasets. A total of 9,631 features were extracted from each protein sequence, and included in a full dimension (FD) RFPDR model. Sequence selection was performed, to generate a reduced-dimension (RD) RFPDR model. Model performances were evaluated using an 80/20 (training/testing) partition, with 10-cross fold validation, and compared to baseline, sequence-based and state-of-the-art strategies. To gain some insights into the underlying biology, the most discriminatory sequence-based features in the RF classifier were identified. RESULTS AND DISCUSSION: RD-RFPDR showed to be sensitive (86.4 ± 4.0%) and specific (96.9 ± 1.5%) for identifying DR proteins, while robust to data imbalance. Its high performance and robustness, added to the fact that RD-RFPDR provides valuable information related to DR proteins underlying properties, make RD-RFPDR an interesting approach for DR protein prediction, complementing the state-of-the-art strategies. |
format | Online Article Text |
id | pubmed-9037127 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-90371272022-04-26 RFPDR: a random forest approach for plant disease resistance protein prediction Simón, Diego Borsani, Omar Filippi, Carla Valeria PeerJ Agricultural Science BACKGROUND: Plant innate immunity relies on a broad repertoire of receptor proteins that can detect pathogens and trigger an effective defense response. Bioinformatic tools based on conserved domain and sequence similarity are within the most popular strategies for protein identification and characterization. However, the multi-domain nature, high sequence diversity and complex evolutionary history of disease resistance (DR) proteins make their prediction a real challenge. Here we present RFPDR, which pioneers the application of Random Forest (RF) for Plant DR protein prediction. METHODS: A recently published collection of experimentally validated DR proteins was used as a positive dataset, while 10x10 nested datasets, ranging from 400-4,000 non-DR proteins, were used as negative datasets. A total of 9,631 features were extracted from each protein sequence, and included in a full dimension (FD) RFPDR model. Sequence selection was performed, to generate a reduced-dimension (RD) RFPDR model. Model performances were evaluated using an 80/20 (training/testing) partition, with 10-cross fold validation, and compared to baseline, sequence-based and state-of-the-art strategies. To gain some insights into the underlying biology, the most discriminatory sequence-based features in the RF classifier were identified. RESULTS AND DISCUSSION: RD-RFPDR showed to be sensitive (86.4 ± 4.0%) and specific (96.9 ± 1.5%) for identifying DR proteins, while robust to data imbalance. Its high performance and robustness, added to the fact that RD-RFPDR provides valuable information related to DR proteins underlying properties, make RD-RFPDR an interesting approach for DR protein prediction, complementing the state-of-the-art strategies. PeerJ Inc. 2022-04-22 /pmc/articles/PMC9037127/ /pubmed/35480565 http://dx.doi.org/10.7717/peerj.11683 Text en ©2022 Simón et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Agricultural Science Simón, Diego Borsani, Omar Filippi, Carla Valeria RFPDR: a random forest approach for plant disease resistance protein prediction |
title | RFPDR: a random forest approach for plant disease resistance protein prediction |
title_full | RFPDR: a random forest approach for plant disease resistance protein prediction |
title_fullStr | RFPDR: a random forest approach for plant disease resistance protein prediction |
title_full_unstemmed | RFPDR: a random forest approach for plant disease resistance protein prediction |
title_short | RFPDR: a random forest approach for plant disease resistance protein prediction |
title_sort | rfpdr: a random forest approach for plant disease resistance protein prediction |
topic | Agricultural Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9037127/ https://www.ncbi.nlm.nih.gov/pubmed/35480565 http://dx.doi.org/10.7717/peerj.11683 |
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