1. Purification and molecular cloning of cDNA for an inducible antibacterial protein of larvae of a coleopteran insect, Holotrichia diomphalia
S Y Lee, H J Moon, S Kurata, T Kurama, S Natori, B L Lee J Biochem. 1994 Jan;115(1):82-6. doi: 10.1093/oxfordjournals.jbchem.a124309.
Injection of Escherichia coli into larvae of the coleopteran Holotrichia diomphalia results in the appearance of antibacterial activity in the hemolymph. An antibacterial protein, named holotricin 2, was purified from larvae of this insect and characterized. A cDNA clone for holotricin 2 was isolated and its complete sequence was determined. This protein was found to inhibit the growth of Gram-negative bacteria and to consist of 72-amino acid residues with no cysteine residues. Its amino acid sequence is similar to that of coleoptericine, an antibacterial protein isolated from larvae of the coleopteran Zophobas atratus.
2. Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin
K Yamada, S Natori Biochem J. 1993 Apr 1;291 ( Pt 1)(Pt 1):275-9. doi: 10.1042/bj2910275.
Two sapecin homologues were purified from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly). These homologues contained six cysteine residues with exactly the same disulphide pairings as those in sapecin. The amino acid sequence of one of them, sapecin C, was also very similar to that of sapecin. The other homologue, sapecin B, was less similar to sapecin but showed significant similarity to charybdotoxin, an inhibitor of K+ channels isolated from a scorpion venom. Like sapecin, these homologues repressed the growth of various Gram-positive bacteria.
3. Purification and cDNA cloning of an antifungal protein from the hemolymph of Holotrichia diomphalia larvae
S Y Lee, H J Moon, S Kurata, S Natori, B L Lee Biol Pharm Bull. 1995 Aug;18(8):1049-52. doi: 10.1248/bpb.18.1049.
An antifungal protein (AFP), holotricin 3, was purified from the hemolymph of the coleopteran insect Holotrichia diomphalia larvae. Analysis of its cDNA showed that holotricin 3 is a novel Gly- and His-rich protein consisting of 84 amino acid residues. This protein was similar to AFP, an antifungal protein of Sarcophaga peregrina that was reported previously, in terms of molecular size and high content of Gly and His residues. However, no appreciable sequence similarity was detected between the two proteins.
