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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
,
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
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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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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