Dietary fulvic acid supplementation improves the growth performance and immune response of sea cucumber (Apostichopus japonicas).

Sea cucumber peptides are small molecular peptides with biological function obtained from fresh sea cucumber as feedstock, which were hydrolyzed by protease, separated ,and purified. As the main product of sea cucumber refinement, it more accurately expresses the nutritional effect of sea cucumber and has a wide range of potential applications. It has been demonstrated that sea cucumber has a certain value-added effect on bone mineral density regulation, but the differences in bone mineral density regulation of extracts from different parts of sea cucumber and the techniques contributing to the efficient isolation of bone sea cucumber peptides have not been reported. Firstly, the aim of this study was to reveal the differences in osteogenic activities of enzymatic peptides from three major parts of sea cucumber: the body wall, the egg protein, and the intestinal protein. Then, the bone-enhancing sea cucumber peptides were isolated based on the characteristics of the dif-ferences in molecular weight distribution, hydrophilicity, and ionisation degree of sea cucumber, and to explore the possible mechanisms of their action. The findings indicated that sea cucumber peptides extracted from three distinct sites exhibited a dose-dependent enhancement of osteoblast proliferation and differentiation. Upon evaluating the three methods of sea cucumber peptide separation based on molecular weight distribution, hydrophilicity, and ionization, it was observed that the fraction isolated by hydrophobicity and 

The Isolation, Purification and Active Mechanism of Sea Cucumber Bone-Strengthening Functional Peptides

Peptidoglycan recognition proteins (PGRPs) represent a key component of the family of pattern recognition receptors (PRRs). The functional mechanisms of PGRPs in innate immunity are poorly understood. In this study, we identified a novel short-type PGRP, AjPGRP-S2, from the sea cucumber Apostichopus japonicus. Our data showed that AjPGRP-S2 encoded an extracellular protein that possessed a signal peptide, a complete zinc (Zn2+) binding site, and a disulfide bond. A recombinant AjPGRP-S2 (rAjPGRP-S2) lacking the signal peptide was generated and demonstrated to exhibit amidase activity. Tissue expression analysis revealed that AjPGRP-S2 was highly expressed in coelomocytes and tube feet. Immune-responsive analysis indicated that AjPGRP-S2 was able to bind to various pathogen-associated molecular patterns (PAMPs) from bacteria and fungi, as well as to Gram-positive and -negative bacteria, and was majorly induced by DAP-PGN challenge. Basing on RNA-Seq and Pearson's correlation testing, RNA interference, and pull-down analysis, AjPGRP-S2 was found to be involved in transducing immune signals to the complement system and other PRRs, such as fibrinogen, by protein interactions to further recognize and kill pathogens. To respond comprehensively against pathogenic invasion, AjPGRP-S2 may also have the potential in transducing immune signals to key processes, such as cell adhesion, nerve conduction, apoptosis, and transcription by complex pathways that have yet to be elucidated. Our findings not only promote our understanding of the immune-related function and mechanisms of the PGRP family in A. japonicus, but also provide important data that will facilitate the identification of key evolutionary characteristics associated with invertebrate PGRPs.

Characterization of a novel short-type peptidoglycan recognition protein from the sea cucumber Apostichopus japonicus

Pattern recognition receptors (PRRs) are the first line of immune defense in invertebrates against pathogen infection; they recognize pathogens and transmit signals to downstream immune pathways. Among these, peptidoglycan recognition proteins (PGRPs) are an important family in invertebrates that generally comprise of complicated isoforms. A comprehensive understanding of PGRPs in evolutionarily and economically important marine invertebrates, such as the sea cucumber, Apostichopus japonicus, is crucial. Previous studies have identified two PGRPs in sea cucumber, AjPGRP-S and AjPGRP-S1, and another novel short-type PGRP, AjPGRP-S3, was additionally identified here. The full-length cDNA sequence of AjPGRP-S3 was obtained here by PCR-RACE, followed by which showed its gene expression analyses by in situ hybridization that showed it to be relatively highly expressed in coelomocytes and tube feet. Based on an analysis of the recombinant protein, rAjPGRP-S3, a board-spectrum pathogen recognition ability was noted that covered diverse Gram-negative and -positive bacteria, and fungi. Moreover, according to the results of yeast two-hybridization, it was suggested that rAJPGRP-S3 interacted with multiple immune-related factors, including proteins involved in the complement system, extracellular matrix, vesicle trafficking, and antioxidant system. These findings prove the important functions of AjPGRP-S3 in the transduction of pathogen signals to downstream immune effectors and help explore the functional differences in the AjPGRP isoforms. 

A novel short-type peptidoglycan recognition protein with unique polysaccharide recognition specificity in sea cucumber, Apostichopus japonicus.

Functions of lysin motif (LysM)-containing protein in antibacterial responses of sea cucumbers, Apostichopus japonicus.

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A novel short-type peptidoglycan recognition protein with unique polysaccharide recognition specificity in sea cucumber, Apostichopus japonicus.

Functions of lysin motif (LysM)-containing protein in antibacterial responses of sea cucumbers, Apostichopus japonicus.