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A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
Published on: July 18, 2013
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SugarBindDB, a resource of glycan-mediated host-pathogen interactions
Julien Mariethoz1, Khaled Khatib2, Davide Alocci3
1Proteome Informatics Group, SIB Swiss Institute of Bioinformatics, Geneva, Switzerland.
Nucleic Acids Research
|November 19, 2015
Summary
The SugarBind Database (SugarBindDB) provides curated data on glycan binding by human pathogen lectins and adhesins. This resource aids in understanding glycan-mediated interactions in pathogenesis.
Area of Science:
- Microbiology
- Biochemistry
- Bioinformatics
Background:
- Pathogenic microorganisms utilize lectins and adhesins to bind host glycans, mediating infection processes.
- Understanding these glycan-protein interactions is crucial for developing novel therapeutic strategies against pathogens.
Purpose of the Study:
- To create a comprehensive, curated database (SugarBindDB) detailing glycan binding by human pathogen lectins and adhesins.
- To provide tools for investigating the functional roles of glycans in pathogen-host interactions.
Main Methods:
- Curated data collection from published literature, focusing on glycan-protein binding pairs.
- Development of a database structure integrating pathogenic agent, lectin/adhesin, and glycan ligand information.
- Implementation of search, navigation, and visualization tools for data exploration.
Main Results:
- SugarBindDB contains curated glycan-protein binding data, with each entry linked to scientific references.
- The database cross-links to external resources like UniProtKB and UniCarbKB for expanded information.
- A substructure search tool enables mapping of glycan ligands and identification of glycan-mediated protein-protein interactions.
Conclusions:
- SugarBindDB serves as a valuable resource for studying glycan binding by human pathogens.
- The database facilitates the discovery of glycan-mediated interactions, potentially revealing new targets for antimicrobial therapies.
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