@article {9276, title = {Comparative Proteome Analysis of Four Stages of Spermatogenesis in the Small-Spotted Catshark (Scyliorhinus canicula)}, journal = {Journal of Proteome Research}, volume = {22}, year = {2023}, month = {Jul-07-2023}, pages = {2477 - 2492}, issn = {1535-3893}, doi = {https://doi.org/10.1021/acs.jproteome.3c00206}, url = {https://pubs.acs.org/doi/10.1021/acs.jproteome.3c00206}, author = {Jeanne, Fabian and Bernay, Beno{\^\i}t and Pascal Sourdaine} } @article {8726, title = {Identification of a New Set of Polypeptidic Sex Pheromones from Cuttlefish (Sepia officinalis)}, journal = {Marine Biotechnology}, year = {2022}, month = {Sep-04-2022}, issn = {1436-2228}, doi = {10.1007/s10126-022-10126-y}, url = {https://link.springer.com/10.1007/s10126-022-10126-y}, author = {C{\'e}line Zatylny-Gaudin and Corre, Erwan and Zanuttini, Bruno and Endress, Maxime and Bernay, Beno{\^\i}t and Pontin, Julien and Leduc, Alexandre and Jo{\"e}l Henry} } @article {8869, title = {Immuno-Enzymatic and Proteomic Approaches for Sexing the African Bonytongue (Heterotis niloticus Cuvier, 1829)}, journal = {Fishes}, volume = {7}, year = {2022}, month = {Jan-06-2022}, pages = {106}, doi = {10.3390/fishes7030106}, url = {https://www.mdpi.com/2410-3888/7/3/106}, author = {Koua, N{\textquoteright}Zi Daniel and Henry, Jo{\"e}l and Corre, Erwan and Pontin, Julien and Bernay, Beno{\^\i}t and N{\'u}{\~n}ez-Rodr{\'\i}guez, Jes{\'u}s} } @article {8725, title = {Multifaceted roles of the egg perivitelline layer in avian reproduction: Functional insights from the proteomes of chicken egg inner and outer sublayers}, journal = {Journal of Proteomics}, volume = {258}, year = {2022}, month = {Jan-04-2022}, pages = {104489}, issn = {18743919}, doi = {10.1016/j.jprot.2022.104489}, url = {https://linkinghub.elsevier.com/retrieve/pii/S1874391922000124}, author = {Br{\'e}geon, M{\'e}gane and Tomas, Daniel and Bernay, Beno{\^\i}t and C{\'e}line Zatylny-Gaudin and Georgeault, Sonia and Labas, Val{\'e}rie and R{\'e}hault-Godbert, Sophie and Guyot, Nicolas} } @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 {9561, title = {Transcriptome Profiling of the Pacific Oyster Crassostrea gigas Visceral Ganglia over a Reproduction Cycle Identifies Novel Regulatory Peptides}, journal = {Marine Drugs}, volume = {19}, year = {2021}, month = {Jan-08-2021}, pages = {452}, doi = {10.3390/md19080452}, url = {https://www.mdpi.com/1660-3397/19/8/452}, author = {R{\'e}alis-Doyelle, Emilie and Schwartz, Julie and Cabau, C{\'e}dric and Le Franc, Lorane and Bernay, Beno{\^\i}t and Guillaume Rivi{\`e}re and Klopp, Christophe and Favrel, Pascal} } @article {8123, title = {Transcriptome Profiling of the Pacific Oyster Visceral Ganglia over a Reproduction Cycle Identifies Novel Regulatory Peptides.}, journal = {Mar Drugs}, volume = {19}, year = {2021}, month = {2021 Aug 07}, abstract = {

The neuropeptides involved in the regulation of reproduction in the Pacific oyster () are quite diverse. To investigate this diversity, a transcriptomic survey of the visceral ganglia (VG) was carried out over an annual reproductive cycle. RNA-seq data from 26 samples corresponding to VG at different stages of reproduction were de novo assembled to generate a specific reference transcriptome of the oyster nervous system and used to identify differentially expressed transcripts. Transcriptome mining led to the identification of novel neuropeptide precursors (NPPs) related to the bilaterian Eclosion Hormone (EH), crustacean female sex hormone/Interleukin 17, Nesfatin, neuroparsin/IGFBP, prokineticins, and urotensin I; to the protostome GNQQN, pleurin, prohormones 3 and 4, prothoracotropic hormones (PTTH), and QSamide/PXXXamide; to the lophotrochozoan CCWamide, CLCCY, HFAamide, and LXRX; and to the mollusk-specific NPPs CCCGS, clionin, FYFY, GNamide, GRWRN, GSWN, GWE, IWMPxxGYxx, LXRYamide, RTLFamide, SLRFamide, and WGAGamide. Among the complete repertoire of NPPs, no sex-biased expression was observed. However, 25 NPPs displayed reproduction stage-specific expression, supporting their involvement in the control of gametogenesis or associated metabolisms.

}, issn = {1660-3397}, doi = {10.3390/md19080452}, author = {R{\'e}alis-Doyelle, Emilie and Schwartz, Julie and Cabau, C{\'e}dric and Le Franc, Lorane and Bernay, Beno{\^\i}t and Riviere, Guillaume and Klopp, Christophe and Favrel, Pascal} } @article {7279, title = {A functional m6 A-RNA methylation pathway in the oyster Crassostrea gigas assumes epitranscriptomic regulation of lophotrochozoan development}, journal = {The FEBS Journal}, year = {2020}, month = {Jan-09-2020}, issn = {1742-464X}, doi = {10.1111/febs.15500}, url = {https://onlinelibrary.wiley.com/doi/abs/10.1111/febs.15500}, author = {Le Franc, Lorane and Bernay, Beno{\^\i}t and Petton, Bruno and Since, Marc and Pascal Favrel and Guillaume Rivi{\`e}re} } @article {7035, title = {Identification and structural characterization of the factors involved in vitellogenesis and its regulation in the African Osteoglossiforme of aquacultural interest Heterotis niloticus (Cuvier, 1829)}, journal = {General and Comparative Endocrinology}, year = {2020}, month = {Jan-06-2020}, pages = {113532}, issn = {00166480}, doi = {10.1016/j.ygcen.2020.113532}, url = {https://linkinghub.elsevier.com/retrieve/pii/S0016648020302859}, author = {Daniel Koua, N{\textquoteright}Zi and Jesus Nu{\~n}ez-Rodriguez and Orjuela, Julie and C{\'e}line Zatylny-Gaudin and Dubos, Marie-Pierre and Bernay, Beno{\^\i}t and Pontin, Julien and Corre, Erwan and Henry, Jo{\"e}l} } @article {7655, title = {-Omic Analysis of the Sepia officinalis White Body: New Insights into Multifunctionality and Haematopoiesis Regulation}, journal = {Journal of Proteome Research}, volume = {19}, year = {2020}, month = {Jul-08-2020}, pages = {3072 - 3087}, issn = {1535-3893}, doi = {10.1021/acs.jproteome.0c0010010.1021/acs.jproteome.0c00100.s00110.1021/acs.jproteome.0c00100.s002}, url = {https://pubs.acs.org/doi/10.1021/acs.jproteome.0c00100}, author = {Benoist, Louis and Corre, Erwan and Bernay, Beno{\^\i}t and Henry, Jo{\"e}l and C{\'e}line Zatylny-Gaudin} } @article {5597, title = {Behavior of Antimicrobial Peptide K4 in a Marine Environment.}, journal = {Probiotics Antimicrob Proteins}, volume = {11}, year = {2019}, pages = {676-686.}, abstract = {

K4 is a de novo peptide with antibacterial activity on human pathogens. It has a short sequence (14 amino acids), with a cationic N-terminal moiety and an amphipathic ɑ-helix structure. The present paper demonstrates its activity on Vibrio bacteria in a marine environment. It was found non-toxic on marine organisms including Artemia salina, Dicentrarchus labrax, and Magallana gigas at different developmental stages, but influenced the growth of unicellular organisms like microalgae, depending on the algal strain and on K4 concentration. Furthermore, an original approach coupling liquid chromatography (RP-HPLC) and mass spectrometry (MS/MS) allowed us to monitor the degradation time course of the peptide for the first time in conditions close to a hatchery environment, i.e., in the presence of oyster spat. We detected truncated forms over time, and the full K4 was gradually no longer found in these filter-feeder oysters. Finally, using an automated optical density meter, we monitored the growth of several aquatic bacteria identified as pathogenic on animals. K4 had a bactericidal effect on Aeromonas salmonicida and Vibrio splendidus LGP32 at concentrations below 45\ μg\ mL-1. Our results show that K4 could be an environment-friendly alternative to antibiotics, non-toxic to several marine organisms. The use of K4 would be particularly useful to decrease the bacterial load associated with food intake in the early developmental stages of marine animals reared in hatcheries

}, doi = {10.1007/s12602-018-9454-3}, author = {Houyvet, Baptiste and Leduc, Alexandre and Cornet, Val{\'e}rie and Pontin, Julien and Bernay, Beno{\^\i}t and Jo{\"e}l Henry and Vetois, Emilie and C{\'e}line Zatylny-Gaudin} } @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 {5439, title = {Identification of a moronecidin-like antimicrobial peptide in the venomous fish Pterois volitans: Functional and structural study of pteroicidin-α.}, journal = {Fish and shellfish Immunology}, year = {2018}, pages = {318-324}, abstract = {

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

}, author = {Houyvet, Baptiste and Yolande Bouchon-Navaro and Bouchon, Claude and Goux, Didier and Bernay, Beno{\^\i}t and Corre, Erwan and C{\'e}line Zatylny-Gaudin} } @article {4626, title = {Molecular characterization of an adipokinetic hormone-related neuropeptide (AKH) from a mollusk}, journal = {General and Comparative Endocrinology}, volume = {243}, year = {2017}, pages = {15-21}, author = {Marie-Pierre Dubos and Bernay, Beno{\^\i}t and Pascal Favrel} } @article {5438, title = {Neuropeptidome of the Cephalopod Sepia officinalis: Identification, Tissue Mapping, and Expression Pattern of Neuropeptides and Neurohormones during Egg Laying.}, journal = {J Proteome Res. }, volume = {15}, year = {2016}, pages = {48-67}, author = {C{\'e}line Zatylny-Gaudin and Cornet, Val{\'e}rie and Leduc, Alexandre and Zanuttini, Bruno and Corre, Erwan and Corguill{\'e}, Gildas Le and Bernay, Beno{\^\i}t and Kraut, Alexandra and Cout{\'e}, Yohan and Jo{\"e}l Henry} } @article {3864, title = {How Egg Case Proteins Can Protect Cuttlefish Offspring?}, journal = {PLoS One}, volume = {10}, year = {2015}, month = {2015}, pages = {e0132836}, abstract = {

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.

}, issn = {1932-6203}, doi = {10.1371/journal.pone.0132836}, author = {Cornet, Val{\'e}rie and Jo{\"e}l Henry and Goux, Didier and Duval, Emilie and Bernay, Beno{\^\i}t and Gildas Le Corguille and Corre, Erwan and C{\'e}line Zatylny-Gaudin} } @article {3626, title = {Molecular characterization of peptide fractions of a Tilapia (Oreochromis niloticus) by-product hydrolysate and in vitro evaluation of antibacterial activity}, journal = {Process Biochemistry}, volume = {50}, year = {2015}, pages = {487-492}, author = {Robert, Marie and C{\'e}line Zatylny-Gaudin and Fournier, Vincent and Corre, Erwan and Gildas Le Corguille and Bernay, Beno{\^\i}t and Jo{\"e}l Henry} } @article {3374, title = {Cellular effects of bacterial N-3-Oxo-dodecanoyl-L-Homoserine lactone on the sponge Suberites domuncula (Olivi, 1792): insights into an intimate inter-kingdom dialogue.}, journal = {PLoS One}, volume = {9}, year = {2014}, month = {2014}, pages = {e97662}, abstract = {

Sponges and bacteria have lived together in complex consortia for 700 million years. As filter feeders, sponges prey on bacteria. Nevertheless, some bacteria are associated with sponges in symbiotic relationships. To enable this association, sponges and bacteria are likely to have developed molecular communication systems. These may include molecules such as N-acyl-L-homoserine lactones, produced by Gram-negative bacteria also within sponges. In this study, we examined the role of N-3-oxododecanoyl-L-homoserine lactone (3-oxo-C12-HSL) on the expression of immune and apoptotic genes of the host sponge Suberites domuncula. This molecule seemed to inhibit the sponge innate immune system through a decrease of the expression of genes coding for proteins sensing the bacterial membrane: a Toll-Like Receptor and a Toll-like Receptor Associated Factor 6 and for an anti-bacterial perforin-like molecule. The expression of the pro-apoptotic caspase-like 3/7 gene decreased as well, whereas the level of mRNA of anti-apoptotic genes Bcl-2 Homolog Proteins did not change. Then, we demonstrated the differential expression of proteins in presence of this 3-oxo-C12-HSL using 3D sponge cell cultures. Proteins involved in the first steps of the endocytosis process were highlighted using the 2D electrophoresis protein separation and the MALDI-TOF/TOF protein characterization: α and β subunits of the lysosomal ATPase, a cognin, cofilins-related proteins and cytoskeleton proteins actin, α tubulin and α actinin. The genetic expression of some of these proteins was subsequently followed. We propose that the 3-oxo-C12-HSL may participate in the tolerance of the sponge apoptotic and immune systems towards the presence of bacteria. Besides, the sponge may sense the 3-oxo-C12-HSL as a molecular evidence of the bacterial presence and/or density in order to regulate the populations of symbiotic bacteria in the sponge. This study is the first report of a bacterial secreted molecule acting on sponge cells and regulating the symbiotic relationship.

}, issn = {1932-6203}, doi = {10.1371/journal.pone.0097662}, author = {Gard{\`e}res, Johan and Jo{\"e}l Henry and Bernay, Beno{\^\i}t and Ritter, Andr{\`e}s and C{\'e}line Zatylny-Gaudin and Wiens, Matthias and M{\"u}ller, Werner E G and Le Pennec, Ga{\"e}l} } @article {3371, title = {Transcriptomic and peptidomic analysis of protein hydrolysates from the white shrimp (L. vannamei).}, journal = {J Biotechnol}, volume = {186}, year = {2014}, month = {2014 Sep 30}, pages = {30-7}, abstract = {

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.

}, issn = {1873-4863}, doi = {10.1016/j.jbiotec.2014.06.020}, author = {Robert, Marie and C{\'e}line Zatylny-Gaudin and Fournier, Vincent and Corre, Erwan and Gildas Le Corguille and Bernay, Beno{\^\i}t and Jo{\"e}l Henry} }