The winged pearl oyster Pteria penguin has the unique stout byssus in comparison with other pearl oysters. However, the mechanism of the byssus secretion in this species has not been largely investigated. This study applied transcriptomic and metabolomic techniques to elucidate this mechanism. The results showed that 3420 differentially expressed genes (DEGs) were identified which were enriched in glycolysis/gluconeogenesis, pentose phosphate pathway, TCA cycle, fatty acid metabolism, mTOR signaling pathway, FoxO signaling pathway and Notch signaling pathway. The metabolomic analysis revealed that 135 significantly different metabolites (SDMs) were identified with 23 pathways involved, including pentose phosphate pathway, glutathione metabolism and amino acid metabolism. Comprehensive analysis of transcriptome and metabolome indicated that glycogen, fatty acid metabolism and protein conversion could be used interchangeably as energy sources. Moreover, the glutathione metabolism and immune response demonstrated the importance of cellular homeostasis for byssus secretion in the winged pearl oyster. Dynamic expression of 5-hydroxytryptamine, dopamine receptors and adenylate cyclase suggested that the foot may regulate byssus secretion through an aminergic neurofeedback system which could translate information into neurochemical signals. In conclusion, this study provided insights into the energy metabolism and signaling regulation of byssus secretion in winged pearl oyster by the transcriptomic and metabolomic analyses.
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http://dx.doi.org/10.1016/j.cbd.2025.101446 | DOI Listing |
Comp Biochem Physiol Part D Genomics Proteomics
June 2025
School of Marine Biology and Fisheries, Hainan University, Haikou 570228, China; State Key Laboratory of Marine Resource Utilization in South China Sea, Hainan University, Haikou 570228, China; Key Laboratory of Tropical Hydrobiology and Biotechnology of Hainan Province, Hainan University, Haikou 570228, China. Electronic address:
The winged pearl oyster Pteria penguin has the unique stout byssus in comparison with other pearl oysters. However, the mechanism of the byssus secretion in this species has not been largely investigated. This study applied transcriptomic and metabolomic techniques to elucidate this mechanism.
View Article and Find Full Text PDFNat Rev Chem
March 2025
Department of Chemistry & Biochemistry, University of California Santa Barbara, Santa Barbara, CA, USA.
Catechol-functionalized proteins in mussel holdfasts are essential for underwater adhesion and cohesion and have inspired countless synthetic polymeric materials and devices. However, as catechols are prone to oxidation, long-term performance and stability of these inventions awaits effective antioxidation strategies. In mussels, catechol-mediated interactions are stabilized by 'built-in' homeostatic redox reservoirs that restore catechols oxidized to quinones.
View Article and Find Full Text PDFBiomacromolecules
February 2025
Department of Chemical Engineering, Pohang University of Science and Technology, Pohang 37673, Republic of Korea.
Mussel byssi form a robust underwater adhesive system, anchoring to various surfaces in harsh marine environments. Central to byssus is foot protein type 4 (fp-4), a junction protein connecting collagenous threads to proteinaceous plaque. This study investigated an anionic plaque-binding domain of fp-4 (fp-4a) and its interactions with cationic foot proteins (fp-1, fp-5, and fp-151 as model substitutes for fp-2) and metal ions (Ca, Fe, and V).
View Article and Find Full Text PDFBiomacromolecules
September 2024
Dept. of Chemistry, McGill University, 801 Sherbrooke Street West, Montreal, Quebec H3A 0B8, Canada.
Marine mussels fabricate tough collagenous fibers known as byssal threads to anchor themselves. Threads are produced individually in minutes via secretion of liquid crystalline (LC) collagenous precursors (preCols); yet the physical and chemical parameters influencing thread formation remain unclear. Here, we characterized the structural anisotropy of native and artificially induced threads using quantitative polarized light microscopy and transmission electron microscopy to elucidate spontaneous vs regulated aspects of thread assembly, discovering that preCol LC phases form aligned domains of several hundred microns, but not the cm-level alignment of native threads.
View Article and Find Full Text PDFJ Proteomics
September 2024
School of Marine Biology and Fisheries, Hainan University, Haikou 570228, China; State Key Laboratory of Marine Resource Utilization in South China Sea, Hainan University, Haikou 570228, China; Key Laboratory of Tropical Hydrobiology and Biotechnology of Hainan Province, Hainan University, Haikou 570228, China. Electronic address:
Byssus is a unique external structure in sessile bivalves and is critical for settlement and metamorphosis. However, little is known about the stout byssus in Pteria penguin. We explored the byssus structure and proteins using scanning electron microscopy and proteomics, respectively.
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