A novel member of lebocin gene family from the silkworm, Bombyx mori.
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 (Leb 3) encoded lebocin 3 and another (Leb 4) is a new member of the lebocin gene family. Gene expression of both Leb 3 and Leb 4 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 in B. mori.
Furukawa
S
S
Laboratory of Applied Zoology, Institute of Agriculture and Forestry, University of Tsukuba, Ibaraki, Japan.
Taniai
K
K
Ishibashi
J
J
Hara
S
S
Shono
T
T
Yamakawa
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry; D001483:Base Sequence; D012831:Bombyx / Q000737:chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D005786:Gene Expression Regulation / Q000187:drug effects; D017344:Genes, Insect; D019476:Insect Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D008070:Lipopolysaccharides / Q000494:pharmacology; D008969:Molecular Sequence Data; D005810:Multigene Family; D009928:Organ Specificity / Q000235:genetics
D000890:Anti-Infective Agents; D019476:Insect Proteins; D008070:Lipopolysaccharides; C095582:lebocin protein, Bombyx mori