RRC ID 41502
Author Okemoto K, Nakajima Y, Fujioka T, Natori S.
Title Participation of two N-terminal residues in LPS-neutralizing activity of sarcotoxin IA.
Journal J Biochem
Abstract Sarcotoxin IA is a cecropin-type antibacterial peptide of flesh fly. Using a mutant sarcotoxin IA lacking two N-terminal residues, we demonstrated that these residues are indispensable for its antibacterial activity against Escherichia coli and LPS-binding. Contrary to the native sarcotoxin IA, the mutant sarcotoxin IA could not neutralize various biological activities of LPS. It was suggested that sarcotoxin IA firmly binds to the lipid A core of LPS via these two N-terminal residues and forms a stable binding complex that exhibits no appreciable biological activity like native LPS.
Volume 131(2)
Pages 277-81
Published 2002-2-1
DOI 10.1093/oxfordjournals.jbchem.a003099
PMID 11820943
MeSH Amino Acids / metabolism Animals Anti-Infective Agents / chemical synthesis Anti-Infective Agents / metabolism* Anti-Infective Agents / pharmacology Blotting, Northern Cells, Cultured Diptera Glucose / metabolism Insect Proteins / genetics Insect Proteins / metabolism* Insect Proteins / pharmacology Lipopolysaccharides / metabolism* Liposomes / metabolism* Macrophages / metabolism Microbial Sensitivity Tests Mutation Neutralization Tests Phospholipids / metabolism RNA / metabolism Tumor Necrosis Factor-alpha / metabolism
IF 2.476
Times Cited 16
Human and Animal Cells