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Volume 272, Number 45, Issue of November 7, 1997 pp. 28398-28406
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

(Received for publication, July 8, 1997, and in revised form, September 11, 1997)

Delphine Destoumieux Dagger , Philippe Bulet § , Damarys Loew par , Alain Van Dorsselaer par , Jenny Rodriguez ** and Evelyne Bachère Dagger

From the Dagger  Institut Français de Recherche et d'Exploitation de la Mer/CNRS, Unité Mixte de Recherche 219, "Défense et Résistance chez les Invertébrés Marins," Université de Montpellier 2, CC 80, 34095 Montpellier, France, the § Institut de Biologie Moléculaire et Cellulaire, Unité Propre de Recherche 9022, CNRS, "Réponse Immunitaire et Développement chez les Insectes," 15 rue René Descartes, 67084 Strasbourg Cedex, France, the par  Laboratoire de Spectrométrie de Masse Bio-Organique, Unité de Recherche Associée 31, CNRS-Université Louis Pasteur, Faculté de Chimie, 1 rue Blaise Pascal, 67008 Strasbourg Cedex, France, and the ** Centro Nacional de Acuiculture e Investigaciones Marinas-Escuela Superior Politécnica del Litoral, Guayaquil, Ecuador

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.


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