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Updated: Jun 22, 2026

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus
Published on: May 31, 2022
Multipeptide precursor structure of acaloleptin A isoforms, antibacterial peptides from the Udo longicorn beetle,
Morikazu Imamura1, Sugino Wada, Kenjiro Ueda
1Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Saiwai-cho, Fuchu, Tokyo 183-8509, Japan.
Abstract:
We previously purified acaloleptin A1, A2, and A3, antibacterial peptides that are produced in the larval hemolymph of Acalolepta luxuriosa (Udo longicorn beetle). In this study, we performed cDNA cloning. The cDNA sequence showed a predicted acaloleptin A precursor that consisted of five acaloleptin A isoforms. Four (isoforms 1, 2, 3 and 4) of the five isoforms of the acaloleptin A precursor had high-level sequence identities with each other, but the N-terminal region of isoform 5 differed from those of the other acaloleptin A isoforms. Northern and Western blot analyses showed that acaloleptin A isoforms were mass-produced soon after bacterial inoculation. Finally, we purified isoform 5 from hemolymph of the immunized larvae. Isoform 5, unlike acaloleptin A1, A2 and A3, showed antimicrobial activities against a Gram-positive bacterium, Micrococcus luteus and a fungus, Magnaporthe grisea. These results suggest that the multipeptide structure of the acaloleptin A precursor allows A. luxuriosa high-level production of antibacterial peptides and resistance to a wide range of microorganisms.
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