@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 {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 {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 {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 {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} }