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Published on: January 26, 2024
PrionScan: an online database of predicted prion domains in complete proteomes
Vladimir Espinosa Angarica1, Alfonso Angulo, Arturo Giner
1Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, Pedro Cerbuna 12, 50009 Zaragoza, Spain. vladimir@espinosa-angarica.com.
Background:
Prions are a particular type of amyloids related to a large variety of important processes in cells, but also responsible for serious diseases in mammals and humans. The number of experimentally characterized prions is still low and corresponds to a handful of examples in microorganisms and mammals. Prion aggregation is mediated by specific protein domains with a remarkable compositional bias towards glutamine/asparagine and against charged residues and prolines. These compositional features have been used to predict new prion proteins in the genomes of different organisms. Despite these efforts, there are only a few available data sources containing prion predictions at a genomic scale.
Description:
Here we present PrionScan, a new database of predicted prion-like domains in complete proteomes. We have previously developed a predictive methodology to identify and score prionogenic stretches in protein sequences. In the present work, we exploit this approach to scan all the protein sequences in public databases and compile a repository containing relevant information of proteins bearing prion-like domains. The database is updated regularly alongside UniprotKB and in its present version contains approximately 28000 predictions in proteins from different functional categories in more than 3200 organisms from all the taxonomic subdivisions. PrionScan can be used in two different ways: database query and analysis of protein sequences submitted by the users. In the first mode, simple queries allow to retrieve a detailed description of the properties of a defined protein. Queries can also be combined to generate more complex and specific searching patterns. In the second mode, users can submit and analyze their own sequences.
Conclusions:
It is expected that this database would provide relevant insights on prion functions and regulation from a genome-wide perspective, allowing researches performing cross-species prion biology studies. Our database might also be useful for guiding experimentalists in the identification of new candidates for further experimental characterization.
Insights
PrionScan is a new database identifying prion-like domains across genomes. This resource aids researchers in studying prion biology and discovering new prion candidates for experimental characterization.
Area of Science:
- Biochemistry
- Genomics
- Proteomics
Background:
- Prions are amyloid proteins implicated in cellular processes and diseases.
- Experimentally characterized prions are limited, hindering comprehensive study.
- Prion domains exhibit specific compositional biases, useful for prediction.
Purpose of the Study:
- To introduce PrionScan, a novel database of predicted prion-like domains in complete proteomes.
- To provide a genomic-scale repository of prion protein predictions.
- To facilitate cross-species prion biology research and experimental candidate identification.
Main Methods:
- Developed and applied a predictive methodology to identify and score prionogenic protein stretches.
- Scanned public protein databases to compile a repository of proteins with prion-like domains.
- Integrated regular updates with UniProtKB for comprehensive proteome coverage.
Main Results:
- Compiled a database with approximately 28,000 predictions in proteins from over 3,200 organisms.
- Included proteins from diverse functional categories across all taxonomic subdivisions.
- Database supports both direct querying and user-submitted sequence analysis.
Conclusions:
- PrionScan offers genome-wide insights into prion functions and regulation.
- Enables cross-species comparative studies in prion biology.
- Aids experimentalists in identifying novel prion candidates for further investigation.
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