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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
Published on: July 25, 2013
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Evolutionary trend of bovine β-defensin proteins toward functionality prediction: A domain-based bioinformatics study
Saiful Islam1, Mst Rubaiat Nazneen Akhand2, Mahmudul Hasan3
1Department of Physiology, Sylhet Agricultural University, Sylhet-3100, Bangladesh.
Heliyon
|March 20, 2023
Summary
Bovine defensins, key innate immune peptides, show diverse evolutionary paths and domain variations. This study reveals their evolutionary relationships and potential specialized functions in cattle immunity.
Area of Science:
- Immunology
- Evolutionary Biology
- Genomics
Background:
- Defensins are crucial cationic peptides in innate immunity with broad antimicrobial and diverse biological functions.
- Limited genomic data and functional analyses exist for bovine beta-defensins, hindering a full understanding of their repertoire and roles.
- The evolutionary divergence and functional adaptation of bovine defensins remain largely unexplored.
Purpose of the Study:
- To investigate the sequence divergence and evolutionary relationships of bovine defensin proteins compared to human counterparts.
- To perform domain-based functional analyses of bovine defensins.
- To elucidate the evolutionary history and potential functional diversification of bovine defensins.
Main Methods:
- Domain-based evolutionary analysis of bovine and human defensin protein sequences.
- Comparative analysis of defensin protein structures, focusing on domain variations and evolutionary clusters.
- Identification of conserved and divergent domains, disulfide bridge patterns, and signature patterns.
Main Results:
- Four major clusters of bovine defensins were identified with significant domain variations, while retaining core antimicrobial activity.
- The beta-defensin domain was identified as the ancestral domain, conserved in cluster I without alpha-helix structures.
- Independent domain evolution occurred in clusters II and III, with some proteins losing domain characteristics; cluster IV contains the most recent domains. Some defensins may have acquired alpha-defensin-like functions.
- Distinct disulfide bridge patterns and signature sequences suggest specialized functions across different tissues.
Conclusions:
- Bovine defensins exhibit significant evolutionary divergence, with distinct clusters reflecting varying degrees of functional adaptation.
- The ancestral beta-defensin domain is conserved, but subsequent evolution has led to diversification and potential acquisition of novel functions.
- Understanding these evolutionary patterns provides insights into the specialized roles of bovine defensins in immunity and host defense against pathogens.
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