TY - JOUR T1 - Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda) A1 - Destoumieux,Delphine A1 - Bulet,Philippe A1 - Loew,Damarys A1 - Van Dorsselaer,Alain A1 - Rodriguez,Jenny A1 - Bachere,Evelyne AD - IFREMER, FRANCE AD - UNIV MONTPELLIER 2, IFREMER, CNRS, F-34095 MONTPELLIER, FRANCE. AD - INST BIOL MOL & CELLULAIRE, CNRS, UPR REPONSE IMMUNITAIRE & DEV CHEZ INSECTES 9022, F-67084 STRASBOURG, FRANCE. AD - UNIV STRASBOURG 1, LAB SPECTROMETRIE MASSE BIOORGAN,URA 31,CNRS, FAC CHIM, F-67008 STRASBOURG, FRANCE. AD - ESCUELA SUPER POLITECN LITORAL, CTR NACL ACUICULTURE & INVEST MARINAS, GUAYAQUIL, ECUADOR. UR - https://archimer.ifremer.fr/doc/00335/44649/ DO - 10.1074/jbc.272.45.28398 N2 - We report here the isolation of three members of a new family of antimicrobial peptides from the hemolymph of shrimps Penaeus vannamei in which immune response has not been experimentally induced. The three molecules display antimicrobial activity against fungi and bacteria with a predominant activity against Gram-positive bacteria. The complete sequences of these peptides were determined by a combination of enzymatic cleavages, Edman degradation, mass spectrometry, and cDNA cloning using a hemocyte cDNA library. The mature molecules (50 and 62 residues) are characterized by an NH2-terminal domain rich in proline residues and a COOH-terminal domain containing three intramolecular disulfide bridges. One of these molecules is post-translationally modified by a pyroglutamic acid at the first position. Comparison of the data obtained from the cDNA clones and mass spectrometry showed that two of these peptides are probably COOH-terminally amidated by elimination of a glycine residue. These molecules with no evident homology to other hitherto described antimicrobial peptides were named penaeidins. Y1 - 1997/11 PB - Amer Soc Biochemistry Molecular Biology Inc JF - Journal Of Biological Chemistry SN - 0021-9258 VL - 272 IS - 45 SP - 28398 EP - 28406 ID - 44649 ER -