@article {8868, title = {Structural and Functional Characterization of Orcokinin B-like Neuropeptides in the Cuttlefish (Sepia officinalis)}, journal = {Marine Drugs}, volume = {20}, year = {2022}, month = {Jan-08-2022}, pages = {505}, doi = {10.3390/md20080505}, url = {https://www.mdpi.com/1660-3397/20/8/505}, author = {Endress, Maxime and C{\'e}line Zatylny-Gaudin and Leprince, J{\'e}r{\^o}me and Lefranc, Benjamin and Corre, Erwan and Le Corguill{\'e}, Gildas and Bernay, Beno{\^\i}t and Leduc, Alexandre and Rangama, Jimmy and Mouret, Liza and Lafont, Anne-Gaelle and Bondon, Arnaud and Jo{\"e}l Henry} } @article {5440, title = {Crustacean cardioactive peptides: Expression, localization, structure, and a possible involvement in regulation of egg-laying in the cuttlefish Sepia officinalis.}, journal = {Gen. Comp. Endocrinol.}, volume = {1}, year = {2018}, pages = {67-79}, abstract = {

The cuttlefish (Sepia officinalis) is a cephalopod mollusk distributed on the western European coast, in the West African Ocean and in the Mediterranean Sea. On the Normandy coast (France), cuttlefish is a target species of professional fishermen, so its reproduction strategy is of particular interest in the context of stock management. Egg-laying, which is coastal, is controlled by several types of regulators among which neuropeptides. The cuttlefish neuropeptidome was recently identified by\ Zatylny-Gaudin\ et al. (2016). Among the 38 neuropeptide families identified, some were significantly overexpressed in egg-laying females as compared to mature males. This study is focused on crustacean cardioactive peptides (CCAPs), a highly expressed neuropeptide family strongly suspected of being involved in the control of egg-laying. We investigated the functional and structural characterization and tissue mapping of CCAPs, as well as the expression patterns of their receptors. CCAPs appeared to be involved in oocyte transport through the oviduct and in mechanical secretion of capsular products. Immunocytochemistry revealed that the neuropeptides were localized throughout the central nervous system (CNS) and in the nerve endings of the glands involved in egg-capsule synthesis and secretion, i.e. the oviduct gland and the main nidamental glands. The CCAP receptor was expressed in these glands and in the subesophageal mass of the CNS. Multiple sequence alignments revealed a high level of conservation of CCAP protein precursors in Sepia officinalis and Loligo pealei, two cephalopod decapods. Primary sequences of CCAPs from the two species were fully conserved, and cryptic peptides detected in the nerve endings were also partially conserved, suggesting biological activity that remains unknown for the time being.

}, doi = {10.1016/j.ygcen.2017.12.009}, author = {Endress, Maxime and C{\'e}line Zatylny-Gaudin and Corre, Erwan and Le Corguill{\'e}, Gildas and Benoist, Louis and Leprince, J{\'e}r{\^o}me and Lefranc, Benjamin and Bernay, Beno{\^\i}t and Leduc, Alexandre and Rangama, Jimmy and Anne-Gaelle Lafont and Bondon, Arnaud and Jo{\"e}l Henry} } @article {5596, title = {Design of antimicrobial peptides from a cuttlefish database.}, journal = {Amino acids}, year = {2018}, abstract = {

No antimicrobial peptide has been identified in cephalopods to date. Annotation of transcriptomes or genomes using basic local alignment Search Tool failed to yield any from sequence identities. Therefore, we searched for antimicrobial sequences in the cuttlefish (Sepia officinalis) database by in silico analysis of a transcriptomic database. Using an original approach based on the analysis of cysteine-free antimicrobial peptides selected from our Antimicrobial Peptide Database (APD3), the online prediction tool of the Collection of Anti-Microbial Peptides (CAMPR3), and a homemade software program, we identified potential antibacterial sequences. Nine peptides less than 25 amino acids long were synthesized. The hydrophobic content of all nine of them ranged from 30 to 70\%, and they could form alpha-helices. Three peptides possessed similarities with piscidins, one with BMAP-27, and five were totally new. Their antibacterial activity was evaluated on eight bacteria including the aquatic pathogens Vibrio alginolyticus, Aeromonas salmonicida, or human pathogens such as Salmonella typhimurium, Listeria monocytogenes, or Staphylococcus aureus. Despite the prediction of an antimicrobial potential for eight of the peptides, only two-GR21\ and KT19-inhibited more than one bacterial strain with minimal inhibitory concentrations below 25\ {\textmu}M. Some sequences like VA20\ and FK19\ were hemolytic, while GR21\ induced less than 10\% of hemolysis on human blood cells at a concentration of 200\ {\textmu}M. GR21\ was the only peptide derived from a precursor with a signal peptide, suggesting a real role in cuttlefish immune defense.

}, doi = {10.1007/s00726-018-2633-4}, author = {Houyvet, Baptiste and Zanuttini, B and Corre, Erwan and Le Corguill{\'e}, Gildas and Jo{\"e}l Henry and C{\'e}line Zatylny-Gaudin} } @article {5499, title = {Dietary aquaculture by-product hydrolysates: impact on the transcriptomic response of the intestinal mucosa of European seabass (Dicentrarchus labrax) fed low fish meal diets}, journal = {BMC Genomics}, volume = {19}, year = {2018}, abstract = {

Aquaculture production is expected to double by 2030, and demands for aquafeeds and raw materials are expected to increase accordingly. Sustainable growth of aquaculture will require the development of highly nutritive and functional raw materials to efficiently replace fish meal. Enzymatic hydrolysis of marine and aquaculture raw materials could bring new functionalities to finished products. The aim of this study was to determine the zootechnical and transcriptomic performances of protein hydrolysates of different origins (tilapia, shrimp, and a combination of the two) in European seabass (Dicentrarchux labrax) fed a low fish meal diet (5\%), for 65\ days.

Results

Results were compared to a positive control fed with 20\% of fish meal. Growth performances, anterior intestine histological organization and transcriptomic responses were monitored and analyzed. Dietary inclusion of protein hydrolysates in the low fish meal diet restored similar growth performances to those of the positive control. Inclusion of dietary shrimp hydrolysate resulted in larger villi and more goblet cells, even better than the positive control. Transcriptomic analysis of the anterior intestine showed that dietary hydrolysate inclusion restored a pattern of intestinal gene expression very close to the pattern of the positive control. However, as compared to the low fish meal diet and depending on their origin, the different hydrolysates did not modulate metabolic pathways in the same way. Dietary shrimp hydrolysate inclusion modulated more metabolic pathways related to immunity, while nutritional metabolism was more impacted by dietary tilapia hydrolysate. Interestingly, the combination of the two hydrolysates enhanced the benefits of hydrolysate inclusion in diets: more genes and metabolic pathways were regulated by the combined hydrolysates than by each hydrolysate tested independently.

Conclusions

Protein hydrolysates manufactured from aquaculture by-products are promising candidates to help replace fish meal in aquaculture feeds without disrupting animal metabolism and performances.

}, keywords = {Aquaculture, Aquafeed, By-products, European seabass, Fishmeal replacement, Hydrolysate, Illumina RNA-sequencing, Intestinal organization, Metabolic pathways}, doi = {doi.org/10.1186/s12864-018-4780-0}, author = {Leduc, Alexandre and C{\'e}line Zatylny-Gaudin and Robert, Marie and Corre, Erwan and Le Corguill{\'e}, Gildas and Castel, H{\'e}l{\`e}ne and Lefevre-Scelles, Antoine and Fournier, Vincent and Gisbert, Enric and Andree, Karl B. and Jo{\"e}l Henry} }