peregrina/antibacterial

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Interaction between liposomes and sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina (flesh fly).

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The direct interaction between phospholipids and sarcotoxin IA, a potent bactericidal protein of Sarcophaga peregrina, was studied using authentic sarcotoxin IA, its synthetic derivatives, and various liposomes. Results showed that sarcotoxin IA interacted with liposomes constituted from acidic

Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina.

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Three antibacterial proteins were purified from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly). Sequencing studies showed that two of these proteins belong to the sarcotoxin I family, potent antibacterial proteins purified from the hemolymph of

Antibacterial activity of a novel 26-kDa serine protease in the yellow body of Sarcophaga peregrina (flesh fly) pupae.

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We have reported a novel serine protease produced by Sarcophaga peregrina (Nakajima et al., J. Biol. Chem. 272 (1997) 23805-23810). This 26-kDa protease showed antibacterial activity against several bacteria. This activity was an intrinsic characteristic of the enzyme protein and not directly

Identification and characterization of an antibacterial peptide of the 26-kDa protease of Sarcophaga peregrina with antibacterial activity.

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Previously, we purified a serine protease with a molecular mass of 26 kDa that exhibits potent antibacterial activity from a pupal extract of Sarcophaga peregrina (flesh fly). We divided this protease into 12 peptides and examined their antibacterial activity. A peptide corresponding to residues 155

Identification of hemagglutinating protein and bactericidal activity in the hemolymph of adult Sarcophaga peregrina on injury of the body wall.

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When the body wall of adult Sarcophaga peregrina (flesh-fly) was injured with a hypodermic needle, hemagglutinating activity and antibacterial activity were induced in the hemolymph simultaneously. The hemagglutinating activity was shown to be due to the same lectin that was found previously in the

Mode of action of a bactericidal protein induced in the haemolymph of Sarcophaga peregrina (flesh-fly) larvae.

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The mode of action of a bactericidal protein (sarcotoxin I) purified from the haemolymph of Sarcophaga peregrina (flesh-fly) larvae was studied, focusing attention on its effect on the function of the membrane of Escherichia coli. Sarcotoxin I almost completely blocked the uptakes of

Molecular cloning of a cDNA and assignment of the C-terminal of sarcotoxin IA, a potent antibacterial protein of Sarcophaga peregrina.

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A previous paper described the complete amino acid sequences of sarcotoxins IA, IB and IC, which are a group of potent antibacterial proteins with almost identical primary structures produced by Sarcophaga peregrina (fleshfly) larvae [Okada & Natori (1985) J. Biol. Chem. 260, 7174-7177]. The present

Characterization of the antimicrobial peptide derived from sapecin B, an antibacterial protein of Sarcophaga peregrina (flesh fly).

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Sapecin B, an antibacterial protein of Sarcophaga peregrina, was divided into four peptides. A hendecapeptide derived from its helix region was found to have comparable antibacterial activity with that of the complete protein. This peptide had a much wider spectrum of antimicrobial activity than

Mode of action of sapecin, a novel antibacterial protein of Sarcophaga peregrina (flesh fly).

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Sapecin is an antibacterial protein purified from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina [Matsuyama, K. & Natori, S. (1988) J. Biol. Chem. 236, 17112-17116]. As this protein inhibited the growth of Gram-positive bacteria better than that of Gram-negative

Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly).

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Sapecin is a 40-residue peptide containing 6 half-cystine residues. The disulfide structure of sapecin was determined by sequencing cystine-containing peptides obtained by digesting sapecin with thermolysin. Results showed that sapecin has a vortical structure fixed by 3 disulfide bonds between

Purification and characterization of N-beta-alanyl-5-S-glutathionyl-3,4-dihydroxyphenylalanine, a novel antibacterial substance of Sarcophaga peregrina (flesh fly).

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We purified a novel antibacterial substance from immunized adult Sarcophaga and determined its molecular structure to be N-beta-alanyl-5-S-glutathionyl-3,4-dihydroxyphenylalanine (5-S-GAD). We synthesized 5-S-GAD enzymatically from N-beta-alanyl-3, 4-dihydroxyphenylalanine (beta-Ala-Dopa) and

Molecular cloning, sequencing, and characterization of cDNA for sarcotoxin IIA, an inducible antibacterial protein of Sarcophaga peregrina (flesh fly).

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A cDNA clone for sarcotoxin IIA, an antibacterial protein of Sarcophaga peregrina (flesh fly) larvae [Ando, K., Okada, M., & Natori, S. (1987) Biochemistry 26, 226-230], was isolated and characterized. Sarcotoxin IIA was found to consist of 270 amino acid residues. Northern blot analysis showed that

Purification of sarcotoxin III, a new antibacterial protein of Sarcophaga peregrina.

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A glycine-rich antibacterial protein with a molecular mass of 7,000 termed sarcotoxin III, was purified to homogeneity from the hemolymph of third instar larvae of Sarcophaga peregrina. When the hemolymph was fractionated, this protein was recovered in the same fraction as sarcotoxin I, a group of

Purification of sarcotoxin II, antibacterial proteins of Sarcophaga peregrina (flesh fly) larvae.

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Three antibacterial proteins with almost identical primary structures termed sarcotoxin IIA, IIB, and IIC were purified to homogeneity from the hemolymph of third instar larvae of Sarcophaga peregrina. The molecular masses of these proteins were about 24,000. These proteins were found to have common

Analysis of a gene cluster for sarcotoxin II, a group of antibacterial proteins of Sarcophaga peregrina.

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Sarcotoxin II is a group of antibacterial proteins of Sarcophaga peregrina (flesh fly) with related primary structures. We have cloned three genes in this family. These genes formed a tandem array with about 2-kb intervals, and one of them was present in the opposite strand. The putative amino acid

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