A Novel Member of Lebocin Gene Family from the Silkworm,Bombyx mori

• Published in: Biochemical and biophysical research communications Vol. 238; no. 3; pp. 769 - 774
• Main Authors: Furukawa, Seiichi, Taniai, Kiyoko, Ishibashi, Jun, Hara, Seiichi, Shono, Toshio, Yamakawa, Minoru
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.09.1997
• Subjects: Amino Acid Sequence; AMINO ACID SEQUENCES; Animals; Anti-Infective Agents - chemistry; Base Sequence; Bombyx - chemistry; Bombyx - genetics; BOMBYX MORI; CHEMICAL COMPOSITION; Cloning, Molecular; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; GENBANK/AB003035; GENBANK/AB003036; Gene Expression Regulation - drug effects; Genes, Insect; Insect Proteins - biosynthesis; Insect Proteins - chemistry; Insect Proteins - genetics; Lipopolysaccharides - pharmacology; MOLECULAR SEQUENCE DATA; Multigene Family; NUCLEOTIDE SEQUENCE; Organ Specificity - genetics; SECUENCIA NUCLEOTIDICA; SEQUENCE NUCLEOTIDIQUE
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1997.7386

We screened genomic clones encoding lebocin, an antibacterial peptide from the silkworm,Bombyx mori.Two positive clones were obtained and their nucleotide sequences indicated that they contain no introns. The deduced amino acid sequences revealed that one clone (Leb3) encoded lebocin 3 and another (Leb4) is a new member of the lebocin gene family. Gene expression of bothLeb3 andLeb4 was shown to be induced by lipopolysaccharide and to occur tissue-specifically in the fat body and hemocytes. Our results suggest that lebocin as well as cecropin forms a multiple gene family inB. mori.