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Titolo:
Purification, characterization and gene expression of a glycine and proline-rich antibacterial protein family from larvae of a beetle, Allomyrina dichotoma
Autore:
Sagisaka, A; Miyanoshita, A; Ishibashi, J; Yamakawa, M;
Indirizzi:
Natl Inst Sericultural & Entomol Sci, Lab Biol Def, Tsukuba, Ibaraki 3058634, Japan Natl Inst Sericultural & Entomol Sci Tsukuba Ibaraki Japan 3058634 Japan
Titolo Testata:
INSECT MOLECULAR BIOLOGY
fascicolo: 4, volume: 10, anno: 2001,
pagine: 293 - 302
SICI:
0962-1075(200108)10:4<293:PCAGEO>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
INSECT DEFENSIN FAMILY; BOMBYX-MORI; INNATE IMMUNITY; ANTIMICROBIAL PEPTIDES; SARCOPHAGA-PEREGRINA; COLEOPTERAN INSECT; CDNA CLONING; CECROPIN-B; DROSOPHILA; SILKWORM;
Keywords:
antibacterial proteins; insect immunity; cDNA; cloning; gene expression; Allomirina dichotoma;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Yamakawa, M Natl Inst Sericultural & Entomol Sci, Lab Biol Def, Tsukuba, Ibaraki 3058634, Japan Natl Inst Sericultural & Entomol Sci Tsukuba IbarakiJapan 3058634
Citazione:
A. Sagisaka et al., "Purification, characterization and gene expression of a glycine and proline-rich antibacterial protein family from larvae of a beetle, Allomyrina dichotoma", INSEC MOL B, 10(4), 2001, pp. 293-302

Abstract

Two structurally related antibacterial proteins were isolated from larvae of a beetle, Allomyrina dichotoma, immunized with Escherichia coil. The twoproteins were designated A. dichotoma (A. d.) coleoptericin A and B. The mature portion of A. d. coleoptericins deduced from nucleotide sequences of the cDNAs consists of seventy-two amino acids without cysteine residues andis rich in glycine (11.1%) and proline (11.1%). Comparison of the amino acid sequences of the A. d. coleoptericins revealed that these antibacterial proteins have 94%, 75%, 50% and 43% similarity to rhinocerosin, holotricin 2, coleoptericin and acaloleptin A1. Recombinant A. d. coleoptericin A and B showed strong antibacterial activity against Staphylococcus aureus, methicillin resistant S. aureus (MRSA) and Bacillus subtilis. Recombinant A. d. coleoptericin A and B were shown to not form pores through bacterial membranes of E. coil, but to hamper cell division. Results of Northern blotting showed that A. d. coleoptericin genes are inducible by bacteria and are expressed strongly in the fat bodies and haemocytes, and weakly in the Malpighian tubules. Analysis of the evolutionary relationship of amino acid sequences among A. d. coleoptericins and other antibacterial proteins suggests that A. d. coleoptericins, rhinocerosin and holotricin 2 are closely related and form a gene family.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/08/20 alle ore 15:29:18