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Diversity and Bioprospection of Functional Proteins from Sea Anemone Heteractis magnifica Based on Multi-Omics Approach
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DOI：10.3390/md24080276.png)
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Abstract
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Sea anemone venom has attracted increasing attention in biomedical research due to its multifarious compounds with biological activities. Although the venom is predominantly made up of proteins, the diversity and complexity of these proteins remain poorly understood. In this work, the proteins derived from the tentacle and column of Heteractis magnifica were investigated by integrating transcriptomic and proteomic technologies. A total of 3573 protein sequences from transcriptome databases were identified and clustered into nine functional categories. We also performed proteomic analysis on the proteins identified in H. magnifica, and 339 proteins were found to be present in both datasets. Notably, a comprehensive analysis of six typical categories was implemented, and the representative proteins were explored in depth using multiple alignments, homology modeling and molecular docking. Meanwhile, a few low-copy but functionally intriguing proteins were discovered, highlighting the presence of unconventional components in sea anemone venom. This work provides the first holistic overview of the typical protein families and novel information on functional proteins from H. magnifica, contributing to a deeper understanding of sea anemone proteins and facilitating the discovery of potential proteins for marine drugs or biotechnological tools.
Keywords:
<i>Heteractis magnifica</i>
functional proteins
transcriptomic
proteomic
AlphaFold3 modeling
molecular docking
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