Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)*
- Delphine Destoumieux‡,
- Philippe Bulet§¶,
- Damarys Loew‖,
- Alain Van Dorsselaer‖,
- Jenny Rodriguez** and
- Evelyne Bachère‡‡
- From the ‡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 ‖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
Abstract
We report here the isolation of three members of a new family of antimicrobial peptides from the hemolymph of shrimpsPenaeus 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.
Footnotes
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↵* This work was supported by the Institut Français de Recherche et d’Exploitation de la Mer and by the Centre National de la Recherche Scientifique.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBank™/EMBL Data Bank with accession number(s) , , , and and to the Swiss-prot Data Base with accession numbers , , , , and .
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↵¶ To whom correspondence regarding isolation and biochemical characterization of antimicrobial peptides should be addressed.
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↵‡ To whom all other correspondence should be addressed. Tel.: 33467144710; Fax: 33467144622.
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↵1 The abbreviations used are: HPLC, high performance liquid chromatography; MALDI-TOF-MS, matrix-assisted laser desorption/ionization-time of flight-mass spectrometry; nanoES-MS-MS, nanoelectrospray ionization tandem mass spectrometry; MIC, minimal inhibitory concentration; PCR, polymerase chain reaction; ORF, open reading frame; MES, 4-morpholinoethanesulfonic acid; ACTH, adrenocorticotropic hormone.
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- Received July 8, 1997.
- Revision received September 11, 1997.
