RRC ID 466
Author Kishimoto K, Fujimoto S, Matsumoto K, Yamano Y, Morishima I.
Title Protein purification, cDNA cloning and gene expression of attacin, an antibacterial protein, from eri-silkworm, Samia cynthia ricini.
Journal Insect Biochem. Mol. Biol.
Abstract Attacin was isolated from immunized larval hemolymph of the wild silkmoth, Samia cynthia ricini. The antibacterial effect of the attacin was limited to some species of Gram-negative bacteria. Two cDNA clones encoding attacin A and B, respectively, were isolated by screening the cDNA library from immunized fat body. The two cDNAs encoded the same length of precursor protein with 233 amino acid residues. The 46-residue prepropeptides of the two attacins were identical to each other, but 4 out of 187 residues of the mature proteins were different in each other. The two attacins show 98% identity at the amino acid level, while 92% identity at the nucleotide level. Both of the mature proteins were highly homologous to cecropia basic attacin with identity of 96%. The attacin transcripts were detected at significant level in fat body, hemocytes and Malpighian tube after injection with peptidoglycan, but not in the midgut and the silkgland. The induction of attacin gene expression was elicited most effectively by peptidoglycan and UV-killed bacteria in the fat body.
Volume 32(8)
Pages 881-7
Published 2002-8
PII S0965174801001771
PMID 12110295
MeSH Amino Acid Sequence Animals Anti-Bacterial Agents / isolation & purification Base Sequence Cloning, Molecular DNA, Complementary / genetics Gene Expression Genes, Insect Insect Proteins / genetics* Insect Proteins / isolation & purification* Molecular Sequence Data Moths / genetics* Moths / metabolism RNA, Messenger / genetics RNA, Messenger / metabolism Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid
IF 3.562
Times Cited 22
WOS Category ENTOMOLOGY BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Silkworms Samia cynthia ricini