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Characterization of a novel antioxidant byssal protein from Mytilus coruscus foot
Xue-Er Wang1, Zhi Liao1, Qiao-Mei Yang1
1Laboratory of Marine Biology Protein Engineering, Marine Science and Technical College, Zhejiang Ocean University, Zhoushan 316022, China.
Abstract:
Mussel byssal proteins are of biomimetic importance for the development of novel underwater bio-adhesive agents. It is important to maintain a reduced state during the process of byssus adhesion. There are 19 mussel foot proteins (MFPs) have been reported in previous studies, among which only MFP-6 had been confirmed as an antioxidant protein in mussel byssus due to the function of cysteines, and playing an essential role in the redox balance of mussel byssus during adhesion process. Although the other four MFPs (MFP-16 ~ MFP-19) also have abundant cysteines, their function is still unknown. In this study, a novel mussel foot protein, named MFP-20, was identified from Mytilus coruscus foot. The sequential features, expression profile, and function of recombinant MFP-20 were verified. The results showed that MFP-20 has more abundant cysteines than other MFPs, the relative expression of mfp-20 was upregulated in Fe3+ stress and low pH seawater. In addition, different adhesive substrates induced significant changes of expression level of mfp-20. Furthermore, rMFP-20 showed strong antioxidant capacity in the DPPH assay, and the abundant cysteines in its sequence may play vital roles in the antioxidation activity. Our findings revealed the possible function of MFP-20 with a totally different sequence from the reported MFP-6 and provided new clues for exploring the redox balance of mussel byssus during the adhesion process.
Insights
Researchers discovered a new mussel foot protein, MFP-20, with abundant cysteines. This protein exhibits strong antioxidant activity, suggesting a key role in maintaining redox balance during mussel adhesion.
Area of Science:
- Biomaterials Science
- Marine Biology
- Biochemistry
Background:
- Mussel byssal proteins are crucial for underwater adhesion, requiring a reduced state.
- Mussel foot protein-6 (MFP-6) is the only known antioxidant protein in mussel byssus, essential for redox balance.
- The function of other cysteine-rich mussel foot proteins (MFPs) remains largely unknown.
Purpose of the Study:
- To identify and characterize a novel mussel foot protein, MFP-20, from Mytilus coruscus.
- To investigate the sequential features, expression profile, and functional role of MFP-20.
- To explore the potential antioxidant function of MFP-20 and its contribution to byssus redox balance.
Main Methods:
- Identification and sequencing of MFP-20 from Mytilus coruscus foot.
- Analysis of recombinant MFP-20 (rMFP-20) for sequential features and antioxidant capacity (DPPH assay).
- Quantitative analysis of mfp-20 expression under various stress conditions (Fe3+ stress, low pH) and on different adhesive substrates.
Main Results:
- MFP-20 possesses a high abundance of cysteine residues, exceeding other known MFPs.
- The expression of mfp-20 was significantly upregulated under Fe3+ stress, low pH, and in response to different adhesive substrates.
- Recombinant MFP-20 demonstrated potent antioxidant activity, with cysteines likely mediating this function.
Conclusions:
- MFP-20 is a novel mussel foot protein with significant antioxidant properties, distinct from MFP-6.
- The abundant cysteines in MFP-20 are crucial for its antioxidant capacity.
- MFP-20 likely plays a vital role in maintaining the redox balance of mussel byssus during adhesion.
