cecropia adenopus/antibacterial

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The antibacterial effect of attacins from the silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli.

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The attacins are antibacterial proteins which accumulate in the hemolymph of the giant silk moth, Hyalophora cecropia, in response to a bacterial infection. Here we show that the permeability barrier function of the outer membrane is affected shortly after addition of attacin to growing cultures of

Insect immunity. 11. Simultaneous induction of antibacterial activity and selection synthesis of some hemolymph proteins in diapausing pupae of Hyalophora cecropia and Samia cynthia.

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We have previously shown that pupae of the giant silkmoth Samia cynthia have a humoral antibacterial activity, which was induced by viable, nonpathogenic gram-negative bacteria (H.G. Boman et al., 1974). We show here that this activity was formed simultaneously with a selective incorporation of

The synthesis of antibacterial proteins in isolated fat body from Cecropia silkmoth pupae.

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Fat body from previously immunized diapausing pupae of the silkmoth, Hyalophora cecropia (Saturniidae), incubated in vitro, released antibacterial activity into the medium and incorporated 3H-leucine into the immunity proteins P1-P9. The release of antibacterial activity from fat body was also

The cecropin locus. Cloning and expression of a gene cluster encoding three antibacterial peptides in Hyalophora cecropia.

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Cecropins A, B, and D are antibacterial peptides of 35-37 amino acids that are synthesized in pupae of the Cecropia moth (Hyalophora cecropia) as a response to a bacterial infection. cDNA cloning has shown that the cecropins are made as preproproteins that are processed in four steps to the mature

The structure of the gene for cecropin B, an antibacterial immune protein from Hyalophora cecropia.

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Pupae of the moth Hyalophora cecropia respond to an injection of live bacteria by the production of a potent antibacterial activity. The broad-spectrum property of this activity is due chiefly to two small proteins, cecropins A and B. Sequences of the proteins showed them to be homologous and to

Insect immunity. The primary structure of the antibacterial protein attacin F and its relation to two native attacins from Hyalophora cecropia.

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The attacins are antibacterial proteins present in the hemolymph of the pupae of the silk moth Hyalophora cecropia after bacterial infection. We present the primary structure of one attacin, the F form. We show that this protein is derived by proteolysis from the native protein, attacin E. Using a

Attacin, an antibacterial protein from Hyalophora cecropia, inhibits synthesis of outer membrane proteins in Escherichia coli by interfering with omp gene transcription.

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Attacins are antibacterial proteins synthesized by pupae of the giant silk moth, Hyalophora cecropia, in response to a bacterial infection. In this report we show that the previously described, attacin-induced alteration in the structure and the permeability of the outer membrane of Escherichia coli

Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae.

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We have investigated low molecular weight antibacterial proteins from the Cecropia moth. Hyalophora cecropia. In addition to the previously described cecropins A and B, five new antibacterial proteins were discovered, the cecropins C, D, E and F, and the factor G. A scheme for the purification of

Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia.

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Six closely related antibacterial proteins, attacins A-F, were isolated from the hemolymph of immunized pupae of the Cecropia moth, Hyalophora cecropia. Chromatofocusing separated attacins A-F, with isoelectric points between 5.7 and 8.3. Immunological experiments show that the attacins constitute

Secondary structure of the cecropins: antibacterial peptides from the moth Hyalophora cecropia.

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Cell-free immunity in Cecropia. A model system for antibacterial proteins.

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Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia.

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Three inducible bacteriolytic proteins, designated P7, P9A and P9B, from the hemolymph of immunized pupae of the giant silk moth Hyalophora cecropia have been purified using a two-step procedure with cation-exchange chromatography. Purified protein P7 has a molecular weight of 15000 and its amino

Molecular cloning, cDNA sequencing, and chemical synthesis of cecropin B from Hyalophora cecropia.

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Two cDNA clones containing coding information for cecropin B from the Cecropia moth (Hyalophora cecropia) were identified by means of a synthetic probe. Sequencing of the two inserts showed that cecropin B is processed from a 62-amino acid residue precursor molecule including a 26-residue leader

On the primary structures of lysozyme, cecropins and attacins from Hyalophora cecropia.

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Diapausing pupae of Cecropia respond to a bacterial infection by the selective synthesis of RNA and 15-20 hemolymph proteins. Of these we have purified lysozyme and two classes of antibacterial proteins called cecropins and attacins. The primary structure has been determined for the lysozyme, one

RNA interference of Hemolin causes depletion of phenoloxidase activity in Hyalophora cecropia.

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Melanization is regulated by the prophenoloxidase cascade and functions as a response to intruding microorganisms in invertebrates. When injecting dsRNA of the lepidopteran immune protein hemolin in pupae of Hyalophora cecropia (Lepidoptera: Saturniidae), we observed a significant reduction in

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