@article {9279, title = {First isolation of Francisella halioticida strains from blue mussel (Mytilus edulis) in Normandy, France}, journal = {Journal of Invertebrate Pathology}, volume = {200}, year = {2023}, month = {09/2023}, pages = {107950}, issn = {00222011}, doi = {10.1016/j.jip.2023.107950}, url = {https://linkinghub.elsevier.com/retrieve/pii/S0022201123000678}, author = {Bouras, H{\'e}l{\`e}ne and Quesnelle, Yann and Barozet, Alix and Goux, Didier and Blin, Jean-Louis and Savary, Manuel and C{\'e}line Zatylny-Gaudin and Maryline Houssin} } @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 {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 {8446, title = {Involvement of RFamide neuropeptides in polyp contraction of the adult scleractinian corals Euphyllia ancora and Stylophora pistillata}, journal = {General and Comparative Endocrinology}, volume = {314}, year = {2021}, month = {Jan-12-2021}, pages = {113905}, issn = {00166480}, doi = {10.1016/j.ygcen.2021.113905}, url = {https://linkinghub.elsevier.com/retrieve/pii/S0016648021001982}, author = {Zhang, Yan and Shikina, Shinya and Ho, Yu-Ying and Chiu, Yi-Ling and I-Chen Yao, Jack and C{\'e}line Zatylny-Gaudin and Sylvie Dufour and Chang, Ching-Fong} } @article {8445, title = {Marine Transcriptomic Analysis for the Identification of New Antimicrobial Peptides}, journal = {Marine Drugs}, volume = {19}, year = {2021}, month = {Jan-09-2021}, pages = {490}, doi = {10.3390/md19090490}, url = {https://www.mdpi.com/1660-3397/19/9/490}, author = {Houyvet, Baptiste and Bouchon-Navaro, Yolande and Bouchon, Claude and Corre, Erwan and C{\'e}line Zatylny-Gaudin} } @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 {7656, title = {In-Depth In Silico Search for Cuttlefish Antimicrobial Peptides Following Bacterial Challenge of Haemocytes}, journal = {Marine Drugs}, volume = {18}, year = {2020}, month = {Jan-09-2020}, pages = {439}, doi = {10.3390/md18090439}, url = {https://www.mdpi.com/1660-3397/18/9/439}, author = {Benoist, Louis and Houyvet, Baptiste and Henry, Jo{\"e}l and Corre, Erwan and Zanuttini, Bruno and C{\'e}line Zatylny-Gaudin} } @article {7023, title = {Involvement of GLWamide neuropeptides in polyp contraction of the adult stony coral Euphyllia ancora}, journal = {Scientific Reports}, volume = {10}, year = {2020}, month = {Jan-12-2020}, abstract = {The existence and function of neurons remain largely unexplored in scleractinian corals. To gain a better understanding of neuronal functions in coral physiology, this study focused on Glycine-Leucine-Tryptophan-amide family neuropeptides (GLWamides), which have been shown to induce muscle contraction and larval metamorphosis in other cnidarians. Molecular identification and functional characterization of GLWamides in the adult stony coral\ Euphyllia ancora\ were performed. We successfully elucidated the full-length cDNA of GLWamide preprohormone in\ E. ancora\ (named EaGLW preprohormone). The deduced amino acid sequence was predicted to contain six potential GLWamide peptides. Tissue distribution analysis demonstrated that transcripts of\ EaGLW preprohormone\ were mainly expressed in the mouth (including the pharynx) and tentacles of the polyps. Immunodetection with an anti-GLWamide monoclonal antibody revealed that GLWamide neurons were mainly distributed in the epidermis of the mouth region and tentacle, in agreement with the distribution patterns of the transcripts. Treatment of the isolated mouth and tentacles with synthetic GLWamide peptides induced the contraction of these isolated tissues. Treatment of polyps with synthetic GLWamide peptides induced the contraction of polyps. These results suggest that GLWamides are involved in polyp contraction (myoactivity) in adult scleractinians. Our data provide new information on the physiological function of neuropeptides in scleractinians.}, doi = {10.1038/s41598-020-66438-3}, url = {http://www.nature.com/articles/s41598-020-66438-3}, author = {Shikina, Shinya and Chiu, Yi-Ling and Zhang, Yan and Yi-ChenYao and Liu, Tai-Yu and Tsai, Pin-Hsuan and C{\'e}line Zatylny-Gaudin and Chang, Ching-Fong} } @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 {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} } @inbook {5441, title = {Egg-Laying in the cuttlefish Sepia officinalis}, booktitle = {Biological Resources of Water}, year = {2018}, issn = {978-1-78923-081-9}, doi = {DOI: 10.5772/intechopen.71915}, author = {C{\'e}line Zatylny-Gaudin and Jo{\"e}l Henry} } @article {5707, title = {Emergence of a cholecystokinin/sulfakinin signalling system in Lophotrochozoa}, journal = {Scientific Reports}, volume = {8}, year = {2018}, month = {11/2018}, pages = {16424}, abstract = {Chordate gastrin/cholecystokinin (G/CCK) and ecdysozoan sulfakinin (SK) signalling systems represent divergent evolutionary scenarios of a common ancestral signalling system. The present article investigates for the first time the evolution of the CCK/SK signalling system in a member of the Lophotrochozoa, the second clade of protostome animals. We identified two G protein-coupled receptors (GPCR) in the oyster\ Crassostrea gigas\ (Mollusca), phylogenetically related to chordate CCK receptors (CCKR) and to ecdysozoan sulfakinin receptors (SKR). These receptors, Cragi-CCKR1 and Cragi-CCKR2, were characterised functionally using a cell-based assay. We identified di- and mono-sulphated forms of oyster Cragi-CCK1 (pEGAWDY(SO3H)DY(SO3H)GLGGGRF-NH2) as the potent endogenous agonists for these receptors. The Cragi-CCK genes were expressed in the visceral ganglia of the nervous system. The Cragi-CCKR1 gene was expressed in a variety of tissues, while Cragi-CCKR2 gene expression was more restricted to nervous tissues. An\ in vitro\ bioassay revealed that different forms of Cragi-CCK1 decreased the frequency of the spontaneous contractions of oyster hindgut. Expression analyses in oysters with contrasted nutritional statuses or in the course of their reproductive cycle highlighted the plausible role of Cragi-CCK signalling in the regulation of feeding and its possible involvement in the coordination of nutrition and energy storage in the gonad. This study confirms the early origin of the CCK/SK signalling system from the common bilaterian ancestor and delivers new insights into its structural and functional evolution in the lophotrochozoan lineage.}, doi = {doi.org/10.1038/s41598-018-34700-4}, url = {https://www.nature.com/articles/s41598-018-34700-4}, author = {Julie Schwartz and Marie-Pierre Dubos and Jeremy Pasquier and C{\'e}line Zatylny-Gaudin and Pascal Favrel} } @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 {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 {3863, title = {The Toll/NF-κB pathway in cuttlefish symbiotic accessory nidamental gland.}, journal = {Dev Comp Immunol}, volume = {53}, year = {2015}, month = {2015 Jul 2}, pages = {42-46}, abstract = {

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.

}, issn = {1879-0089}, doi = {10.1016/j.dci.2015.06.016}, author = {Cornet, Val{\'e}rie and Jo{\"e}l Henry and Corre, Erwan and Gildas Le Corguille and C{\'e}line Zatylny-Gaudin} } @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 {3373, title = {Diversity of the RFamide peptide family in mollusks}, journal = {frontiers in endocrinology}, volume = {5}, year = {2014}, type = {review}, abstract = {

Since the initial characterization of the cardioexcitatory peptide FMRFamide in the bivalve
mollusk Macrocallista nimbosa, a great number of FMRFamide-like peptides (FLPs) have
been identified in mollusks. FLPs were initially isolated and molecularly characterized in
model mollusks using biochemical methods. The development of recombinant technologies
and, more recently, of genomics has boosted knowledge on their diversity in various
mollusk classes. Today, mollusk FLPs represent approximately 75 distinct RFamide peptides
that appear to result from the expression of only five genes: the FMRFamide-related
peptide gene, the LFRFamide gene, the luqin gene, the neuropeptide F gene, and the cholecystokinin/
sulfakinin gene. FLPs display a complex spatiotemporal pattern of expression
in the central and peripheral nervous system.Working as neurotransmitters, neuromodulators,
or neurohormones, FLPs are involved in the control of a great variety of biological
and physiological processes including cardiovascular regulation, osmoregulation, reproduction,
digestion, and feeding behavior. From an evolutionary viewpoint, the major challenge
will then logically concern the elucidation of the FLP repertoire of orphan mollusk classes
and the way they are functionally related. In this respect, deciphering FLP signaling pathways
by characterizing the specific receptors these peptides bind remains another exciting
objective.

}, author = {C{\'e}line Zatylny-Gaudin and Pascal Favrel} } @article {3368, title = {Dual role of the cuttlefish salivary proteome in defense and predation.}, journal = {J Proteomics}, volume = {108}, year = {2014}, month = {2014 Aug 28}, pages = {209-22}, abstract = {

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{\textquoteright} 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.

}, issn = {1876-7737}, doi = {10.1016/j.jprot.2014.05.019}, author = {Cornet, Val{\'e}rie and Jo{\"e}l Henry and Corre, Erwan and Gildas Le Corguille and Zanuttini, Bruno and C{\'e}line Zatylny-Gaudin} } @article {3370, title = {Protecting honey bees: identification of a new varroacide by in silico, in vitro, and in vivo studies.}, journal = {Parasitol Res}, volume = {113}, year = {2014}, month = {2014 Dec}, pages = {4601-10}, abstract = {

Varroa destructor is the main concern related to the gradual decline of honeybees. Nowadays, among the various acaricides used in the control of V. destructor, most presents increasing resistance. An interesting alternative could be the identification of existent molecules as new acaricides with no effect on honeybee health. We have previously constructed the first 3D model of AChE for honeybee. By analyzing data concerning amino acid mutations implicated in the resistance associated to pesticides, it appears that pirimicarb should be a good candidate for varroacide. To check this hypothesis, we characterized the AChE gene of V. destructor. In the same way, we proposed a 3D model for the AChE of V. destructor. Starting from the definition of these two 3D models of AChE in honeybee and varroa, a comparison between the gorges of the active site highlighted some major differences and particularly different shapes. Following this result, docking studies have shown that pirimicarb adopts two distinct positions with the strongest intermolecular interactions with VdAChE. This result was confirmed with in vitro and in vivo data for which a clear inhibition of VdAChE by pirimicarb at 10 μM (contrary to HbAChE) and a 100\% mortality of varroa (dose corresponding to the LD50 (contact) for honeybee divided by a factor 100) were observed. These results demonstrate that primicarb could be a new varroacide candidate and reinforce the high relationships between in silico, in vitro, and in vivo data for the design of new selective pesticides.

}, issn = {1432-1955}, doi = {10.1007/s00436-014-4150-z}, author = {Dulin, Fabienne and C{\'e}line Zatylny-Gaudin and Ballandonne, C{\'e}line and Guillet, Bertrand and Bonafos, Romain and Bureau, Ronan and Halm, Marie Pierre} } @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} }