%0 Journal Article %J Marine Biotechnology %D 2022 %T Identification of a New Set of Polypeptidic Sex Pheromones from Cuttlefish (Sepia officinalis) %A Céline Zatylny-Gaudin %A Corre, Erwan %A Zanuttini, Bruno %A Endress, Maxime %A Bernay, Benoît %A Pontin, Julien %A Leduc, Alexandre %A Joël Henry %B Marine Biotechnology %8 Sep-04-2022 %G eng %U https://link.springer.com/10.1007/s10126-022-10126-y %! Mar Biotechnol %R 10.1007/s10126-022-10126-y %0 Journal Article %J Fishes %D 2022 %T Immuno-Enzymatic and Proteomic Approaches for Sexing the African Bonytongue (Heterotis niloticus Cuvier, 1829) %A Koua, N’Zi Daniel %A Henry, Joël %A Corre, Erwan %A Pontin, Julien %A Bernay, Benoît %A Núñez-Rodríguez, Jesús %B Fishes %V 7 %P 106 %8 Jan-06-2022 %G eng %U https://www.mdpi.com/2410-3888/7/3/106 %N 3 %! Fishes %R 10.3390/fishes7030106 %0 Journal Article %J Marine Drugs %D 2022 %T Structural and Functional Characterization of Orcokinin B-like Neuropeptides in the Cuttlefish (Sepia officinalis) %A Endress, Maxime %A Céline Zatylny-Gaudin %A Leprince, Jérôme %A Lefranc, Benjamin %A Corre, Erwan %A Le Corguillé, Gildas %A Bernay, Benoît %A Leduc, Alexandre %A Rangama, Jimmy %A Mouret, Liza %A Lafont, Anne-Gaelle %A Bondon, Arnaud %A Joël Henry %B Marine Drugs %V 20 %P 505 %8 Jan-08-2022 %G eng %U https://www.mdpi.com/1660-3397/20/8/505 %N 8 %! Marine Drugs %R 10.3390/md20080505 %0 Journal Article %J Marine Drugs %D 2021 %T Marine Transcriptomic Analysis for the Identification of New Antimicrobial Peptides %A Houyvet, Baptiste %A Bouchon-Navaro, Yolande %A Bouchon, Claude %A Corre, Erwan %A Céline Zatylny-Gaudin %B Marine Drugs %V 19 %P 490 %8 Jan-09-2021 %G eng %U https://www.mdpi.com/1660-3397/19/9/490 %N 9 %! Marine Drugs %R 10.3390/md19090490 %0 Journal Article %J Frontiers in Physiology %D 2020 %T Diversity of Light Sensing Molecules and Their Expression During the Embryogenesis of the Cuttlefish (Sepia officinalis) %A Bonadè, Morgane %A Ogura, Atsushi %A Corre, Erwan %A Bassaglia, Yann %A Laure Bonnaud-Ponticelli %K arrestin %K cryptochrome %K Development %K Eye %K opsin %K Sepia officinalis %B Frontiers in Physiology %V 11 %P 521989 %G eng %U https://hal.sorbonne-universite.fr/hal-02989850 %R 10.3389/fphys.2020.521989 %0 Journal Article %J General and Comparative Endocrinology %D 2020 %T Identification and structural characterization of the factors involved in vitellogenesis and its regulation in the African Osteoglossiforme of aquacultural interest Heterotis niloticus (Cuvier, 1829) %A Daniel Koua, N'Zi %A Jesus Nuñez-Rodriguez %A Orjuela, Julie %A Céline Zatylny-Gaudin %A Dubos, Marie-Pierre %A Bernay, Benoît %A Pontin, Julien %A Corre, Erwan %A Henry, Joël %B General and Comparative Endocrinology %P 113532 %8 Jan-06-2020 %G eng %U https://linkinghub.elsevier.com/retrieve/pii/S0016648020302859 %! General and Comparative Endocrinology %R 10.1016/j.ygcen.2020.113532 %0 Journal Article %J Marine Drugs %D 2020 %T In-Depth In Silico Search for Cuttlefish Antimicrobial Peptides Following Bacterial Challenge of Haemocytes %A Benoist, Louis %A Houyvet, Baptiste %A Henry, Joël %A Corre, Erwan %A Zanuttini, Bruno %A Céline Zatylny-Gaudin %B Marine Drugs %V 18 %P 439 %8 Jan-09-2020 %G eng %U https://www.mdpi.com/1660-3397/18/9/439 %N 9 %! Marine Drugs %R 10.3390/md18090439 %0 Journal Article %J Journal of Proteome Research %D 2020 %T -Omic Analysis of the Sepia officinalis White Body: New Insights into Multifunctionality and Haematopoiesis Regulation %A Benoist, Louis %A Corre, Erwan %A Bernay, Benoît %A Henry, Joël %A Céline Zatylny-Gaudin %B Journal of Proteome Research %V 19 %P 3072 - 3087 %8 Jul-08-2020 %G eng %U https://pubs.acs.org/doi/10.1021/acs.jproteome.0c00100 %N 8 %! J. Proteome Res. %R 10.1021/acs.jproteome.0c0010010.1021/acs.jproteome.0c00100.s00110.1021/acs.jproteome.0c00100.s002 %0 Journal Article %J Gen. Comp. Endocrinol. %D 2018 %T Crustacean cardioactive peptides: Expression, localization, structure, and a possible involvement in regulation of egg-laying in the cuttlefish Sepia officinalis. %A Endress, Maxime %A Céline Zatylny-Gaudin %A Corre, Erwan %A Le Corguillé, Gildas %A Benoist, Louis %A Leprince, Jérôme %A Lefranc, Benjamin %A Bernay, Benoît %A Leduc, Alexandre %A Rangama, Jimmy %A Anne-Gaelle Lafont %A Bondon, Arnaud %A Joël Henry %X

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.

%B Gen. Comp. Endocrinol. %V 1 %P 67-79 %G eng %N 260 %R 10.1016/j.ygcen.2017.12.009 %0 Journal Article %J Amino acids %D 2018 %T Design of antimicrobial peptides from a cuttlefish database. %A Houyvet, Baptiste %A Zanuttini, B %A Corre, Erwan %A Le Corguillé, Gildas %A Joël Henry %A Céline Zatylny-Gaudin %X

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 µM. 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 µM. GR21 was the only peptide derived from a precursor with a signal peptide, suggesting a real role in cuttlefish immune defense.

%B Amino acids %G eng %R 10.1007/s00726-018-2633-4 %0 Journal Article %J BMC Genomics %D 2018 %T Dietary aquaculture by-product hydrolysates: impact on the transcriptomic response of the intestinal mucosa of European seabass (Dicentrarchus labrax) fed low fish meal diets %A Leduc, Alexandre %A Céline Zatylny-Gaudin %A Robert, Marie %A Corre, Erwan %A Le Corguillé, Gildas %A Castel, Hélène %A Lefevre-Scelles, Antoine %A Fournier, Vincent %A Gisbert, Enric %A Andree, Karl B. %A Joël Henry %K Aquaculture %K Aquafeed %K By-products %K European seabass %K Fishmeal replacement %K Hydrolysate %K Illumina RNA-sequencing %K Intestinal organization %K Metabolic pathways %X

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.

%B BMC Genomics %V 19 %G eng %N 396 %R doi.org/10.1186/s12864-018-4780-0 %0 Journal Article %J Fish and shellfish Immunology %D 2018 %T Identification of a moronecidin-like antimicrobial peptide in the venomous fish Pterois volitans: Functional and structural study of pteroicidin-α. %A Houyvet, Baptiste %A Yolande Bouchon-Navaro %A Bouchon, Claude %A Goux, Didier %A Bernay, Benoît %A Corre, Erwan %A Céline Zatylny-Gaudin %X

The present study characterizes for the first time an antimicrobial peptide in lionfish (Pterois volitans), a venomous fish. Using a peptidomic approach, we identified a mature piscidin in lionfish and called it pteroicidin-α. We detected an amidated form (pteroicidin-α- CONH2) and a non-amidated form (pteroicidin-α-COOH), and then performed their functional and structural study. Interestingly, the two peptides displayed different antibacterial and hemolytic activity levels. Pteroicidin-α-CONH2 was bactericidal on human pathogens like Staphylococcus aureus or Escherichia coli, as well as on the fish pathogen Aeromonas salmonicida, while pteroicidin-α-COOH only inhibited their growth. Furthermore, the two peptides induced hemolysis of red blood cells from different vertebrates, namely humans, sea bass and lesser-spotted dogfish. Hemolysis occurred with low concentrations of pteroicidin-α-CONH2, indicating greater toxicity of the amidated form. Circular dichroism analysis showed that both peptides adopted a helical conformation, yet with a greater α-helix content in pteroicidin-α-CONH2. Overall, these results suggest that amidation strongly influences pteroicidin-α by modifying its structure and its physico-chemical characteristics and by increasing its hemolytic activity

%B Fish and shellfish Immunology %P 318-324 %G eng %N 72 %0 Journal Article %J Environmental Microbiology %D 2017 %T Physiological adjustments and transcriptome reprogramming are involved in the acclimation to salinity gradients in diatoms %A Adrien Bussard %A Corre, Erwan %A Cédric Hubas %A Duvernois‐Berthet, Evelyne %A Gildas Le Corguille %A Jourdren, Laurent %A Coulpier, Fanny %A Pascal Claquin %A Pascal Jean Lopez %X

Salinity regimes in estuaries and coastal areas vary with river discharge patterns, seawater evaporation, the morphology of the coastal waterways, and the dynamics of marine water mixing. Therefore, microalgae have to respond to salinity variations at time scales ranging from daily to annual cycles. Microalgae may also have to adapt to physical alterations that induce the loss of connectivity between habitats and the enclosure of bodies of water. Here, we integrated physiological assays and measurements of morphological plasticity with a functional genomics approach to examine the regulatory changes that occur during the acclimation to salinity in the estuarine diatom Thalassiosira weissflogii. We found that cells exposed to different salinity regimes for a short or long period presented adjustments in their carbon fractions, silicon pools, pigment concentrations and/or photosynthetic parameters. Salinity-induced alterations in frustule symmetry were observed only in the long-term cultures. Whole transcriptome analyses revealed a down-regulation of nuclear and plastid encoded genes during the long-term response and identified only a few regulated genes that were in common between the short- and long-term responses. We propose that in diatoms, one strategy for acclimating to salinity gradients and maintaining optimal cellular fitness could be a reduction in the cost of transcription. This article is protected by copyright. All rights reserved.

%B Environmental Microbiology %V 19 %P 909-925 %8 5 %G eng %U http://dx.doi.org/10.1111/1462-2920.13398 %N 3 %R 10.1111/1462-2920.13398 %0 Journal Article %J J Proteome Res. %D 2016 %T Neuropeptidome of the Cephalopod Sepia officinalis: Identification, Tissue Mapping, and Expression Pattern of Neuropeptides and Neurohormones during Egg Laying. %A Céline Zatylny-Gaudin %A Cornet, Valérie %A Leduc, Alexandre %A Zanuttini, Bruno %A Corre, Erwan %A Corguillé, Gildas Le %A Bernay, Benoît %A Kraut, Alexandra %A Couté, Yohan %A Joël Henry %B J Proteome Res. %V 15 %P 48-67 %G eng %N 1 %0 Journal Article %J PLoS One %D 2015 %T Diversification, Evolution and Sub-Functionalization of 70kDa Heat-Shock Proteins in Two Sister Species of Antarctic Krill: Differences in Thermal Habitats, Responses and Implications under Climate Change. %A Cascella, Kévin %A Jollivet, Didier %A Papot, Claire %A Nelly Léger %A Corre, Erwan %A Juliette Ravaux %A Clark, Melody S %A Toullec, Jean-Yves %X

BACKGROUND: A comparative thermal tolerance study was undertaken on two sister species of Euphausiids (Antarctic krills) Euphausia superba and Euphausia crystallorophias. Both are essential components of the Southern Ocean ecosystem, but occupy distinct environmental geographical locations with slightly different temperature regimes. They therefore provide a useful model system for the investigation of adaptations to thermal tolerance.

METHODOLOGY/PRINCIPAL FINDING: Initial CTmax studies showed that E. superba was slightly more thermotolerant than E. crystallorophias. Five Hsp70 mRNAs were characterized from the RNAseq data of both species and subsequent expression kinetics studies revealed notable differences in induction of each of the 5 orthologues between the two species, with E. crystallorophias reacting more rapidly than E. superba. Furthermore, analyses conducted to estimate the evolutionary rates and selection strengths acting on each gene tended to support the hypothesis that diversifying selection has contributed to the diversification of this gene family, and led to the selective relaxation on the inducible C form with its possible loss of function in the two krill species.

CONCLUSIONS: The sensitivity of the epipelagic species E. crystallorophias to temperature variations and/or its adaptation to cold is enhanced when compared with its sister species, E. superba. These results indicate that ice krill could be the first of the two species to be impacted by the warming of coastal waters of the Austral ocean in the coming years due to climate change.

%B PLoS One %V 10 %P e0121642 %8 2015 %G eng %N 4 %R 10.1371/journal.pone.0121642 %0 Journal Article %J PLoS One %D 2015 %T How Egg Case Proteins Can Protect Cuttlefish Offspring? %A Cornet, Valérie %A Joël Henry %A Goux, Didier %A Duval, Emilie %A Bernay, Benoît %A Gildas Le Corguille %A Corre, Erwan %A Céline Zatylny-Gaudin %X

Sepia officinalis egg protection is ensured by a complex capsule produced by the female accessory genital glands and the ink bag. Our study is focused on the proteins constituting the main egg case. De novo transcriptomes from female genital glands provided essential databases for protein identification. A proteomic approach in SDS-PAGE coupled with MS unveiled a new egg case protein family: SepECPs, for Sepia officinalis Egg Case Proteins. N-glycosylation was demonstrated by PAS staining SDS-PAGE gels. These glycoproteins are mainly produced in the main nidamental glands. SepECPs share high sequence homology, especially in the signal peptide and the three cysteine-rich domains. SepECPs have a high number of cysteines, with conserved motifs involved in 3D-structure. SDS-PAGE showed that SepECPs could form dimers; this result was confirmed by TEM observations, which also revealed a protein network. This network is similar to the capsule network, and it associates these structural proteins with polysaccharides, melanin and bacteria to form a tight mesh. Its hardness and elasticity provide physical protection to the embryo. In addition, SepECPs also have bacteriostatic antimicrobial activity on GRAM- bacteria. By observing the SepECP / Vibrio aestuarianus complex in SEM, we demonstrated the ability of these proteins to agglomerate bacteria and thus inhibit their growth. These original proteins identified from the outer egg case ensure the survival of the species by providing physical and chemical protection to the embryos released in the environment without any maternal protection.

%B PLoS One %V 10 %P e0132836 %8 2015 %G eng %N 7 %R 10.1371/journal.pone.0132836 %0 Journal Article %J Process Biochemistry %D 2015 %T Molecular characterization of peptide fractions of a Tilapia (Oreochromis niloticus) by-product hydrolysate and in vitro evaluation of antibacterial activity %A Robert, Marie %A Céline Zatylny-Gaudin %A Fournier, Vincent %A Corre, Erwan %A Gildas Le Corguille %A Bernay, Benoît %A Joël Henry %B Process Biochemistry %V 50 %P 487-492 %G eng %N 3 %0 Journal Article %J Dev Comp Immunol %D 2015 %T The Toll/NF-κB pathway in cuttlefish symbiotic accessory nidamental gland. %A Cornet, Valérie %A Joël Henry %A Corre, Erwan %A Gildas Le Corguille %A Céline Zatylny-Gaudin %X

The female genital apparatus of decapod cephalopods contains a symbiotic accessory nidamental gland (ANG) that harbors bacterial symbionts. Although the ANG bacterial consortium is now well described, the impact of symbiosis on Sepia officinalis innate immunity pathways remains unknown. In silico analysis of the de novo transcriptome of ANG highlighted for the first time the existence of the NF-κB pathway in S. officinalis. Several signaling components were identified, i.e. five Toll-like receptors, eight signaling cascade features, and the immune response target gene iNOS, previously described as being involved in the initiation of bacterial symbiosis in a cephalopod gland. This work provides a first key for studying bacterial symbiosis and its impact on innate immunity in S. officinalis ANG.

%B Dev Comp Immunol %V 53 %P 42-46 %8 2015 Jul 2 %G eng %N 1 %R 10.1016/j.dci.2015.06.016 %0 Journal Article %J J Proteomics %D 2014 %T Dual role of the cuttlefish salivary proteome in defense and predation. %A Cornet, Valérie %A Joël Henry %A Corre, Erwan %A Gildas Le Corguille %A Zanuttini, Bruno %A Céline Zatylny-Gaudin %X

UNLABELLED: We characterized the proteome of the posterior salivary glands of the cephalopod S. officinalis by combining de novo RNA sequencing and mass spectrometry. In silico analysis of the transcriptome revealed the occurrence of three main categories of proteins: enzymes, immune factors and toxins. Protein identification by SDS-PAGE and MALDI-TOF/TOF confirmed the occurrence of proteins essential to venom-like enzymes: peptidase S1 under four isoforms, phospholipase A2 and two toxins. The first toxin is a cystein rich secreted protein (CRISP), a common toxin found in all venomous animals. The second one is cephalotoxin, which is specific to decabrachia cephalopods. Secretions of the posterior salivary glands are transported to the cephalopodium; they are involved in prey catching but also in gamete storage, fertilization and egg-laying. The paralyzing activity and the antimicrobial effect of saliva suggest a dual role in predation and in immune defense in cuttlefish.

BIOLOGICAL SIGNIFICANCE: The originality of this study lies in the use of a transcriptomic approach (de novo RNA sequencing) coupled to a proteomic approach to get an overview of posterior salivary glands in S. officinalis. In cephalopods, these glands are involved in predation, more precisely in paralyzing preys and digesting them. Our in silico analysis equally reveals a role in immune defense as observed in mammals' saliva. Our study also shows the specificity of cuttlefish venom, with the identification of cephalotoxins, proteins that are not found in octopuses. Finally, we show that cuttlefish saliva is a complex mixture that has antibacterial and crippling properties, but no lethal effect.

%B J Proteomics %V 108 %P 209-22 %8 2014 Aug 28 %G eng %1 http://www.ncbi.nlm.nih.gov/pubmed/24892799?dopt=Abstract %R 10.1016/j.jprot.2014.05.019 %0 Journal Article %J J Biotechnol %D 2014 %T Transcriptomic and peptidomic analysis of protein hydrolysates from the white shrimp (L. vannamei). %A Robert, Marie %A Céline Zatylny-Gaudin %A Fournier, Vincent %A Corre, Erwan %A Gildas Le Corguille %A Bernay, Benoît %A Joël Henry %X

An RNAseq approach associated to mass spectrometry was conducted to assess the composition, molecular mass distribution and primary sequence of hydrolytic peptides issued from hydrolysates of white shrimp (Litopenaeus vannamei) by-products. High performance size exclusion chromatography (HPSEC) analyses indicated that 69.2% of the 214-nm-absorbing components had apparent molecular masses below 1000 Da, and 88.3% below 2000 Da. OFFGEL-nLC-MALDI-TOF/TOF and nLC-ESI-MS/MS analyses led to the identification of 808 peptides based on the NCBI EST databank (161,397 entries) completed by the new L. vannamei databank (58,508 entries) that we created from the RNAs of tissues used for hydrolysate production. Whereas most of hydrolytic peptides have a MW below 2000 Da, preliminary investigations of antimicrobial properties revealed three antibacterial fractions that demonstrate functional activities. The abundance of small peptides as well as the biological activities detected could imply very interesting applications for shrimp hydrolysate in the field of aquaculture feeding.

%B J Biotechnol %V 186 %P 30-7 %8 2014 Sep 30 %G eng %1 http://www.ncbi.nlm.nih.gov/pubmed/24998765?dopt=Abstract %R 10.1016/j.jbiotec.2014.06.020