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Acaloleptins A: Inducible antibacterial peptides from larvae of the beetle, Acalolepta luxuriosa
Author(s) -
Imamura Morikazu,
Wada Sugino,
Koizumi Nobuo,
Kadotani Tomoyuki,
Yaoi Katsuro,
Sato Ryoichi,
Iwahana Hidenori
Publication year - 1999
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1999)40:2<88::aid-arch3>3.0.co;2-b
Subject(s) - hemolymph , biology , antibacterial activity , peptide sequence , biochemistry , insect , amino acid , bacteria , antibacterial peptide , peptide , molecular mass , botany , enzyme , gene , genetics
We purified and characterized three structurally related antibacterial peptides with a molecular mass of 8 kDa (acaloleptins A1, A2, and A3) from the hemolymph of immunized larvae of the Udo longicorn beetle, Acalolepta luxuriosa . These peptides have the same 6 N‐terminal amino acid residues and show potent antibacterial activity against some Gram‐negative bacteria. The three peptides are thought to be isoforms. Reverse phase HPLC analysis of the hemolymph of immunized and naive larvae showed that acaloleptins A1, A2, and A3 were inducible and suggested that all three peptides were produced in a single insect. We determined the complete amino acid sequence of acaloleptin A1. Acaloleptin A1 consists of 71 amino acid residues and shares significant sequence similarity with coleoptericin and holotricin 2, which were isolated from other coleopteran insects. Furthermore, the 29 C‐terminal residues of acaloleptin A1 had 40% identity with the 30 C‐terminal residues of hymenoptaecin found in honeybees. Arch. Insect Biochem. Physiol. 40:88–98, 1999. © 1999 Wiley‐Liss, Inc.