@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 {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 {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 {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} }