cDNA cloning of the neutrophil bactericidal peptide indolicidin.
A structurally novel, tryptophan-rich antimicrobial tridecapeptide amide, named indolicidin, has recently been purified from bovine neutrophils (Selsted et al. (1992) J. Biol. Chem. 267, 4292-4295). Here we describe the molecular cloning of this endoantibiotic, which is synthesised in bone marrow cells as a 144 amino acid residue precursor. The encoded protein has a predicted mass of 16479 Da and a pI of 6.51. A putative signal peptide of 29 amino acids precedes a 101 residue pro-region. The mature peptide is at the 3' end of the open reading frame. A glycine, not found in purified indolicidin, is present at the carboxyl terminus of the deduced sequence and is very likely involved in post-translational peptide amidation.
Del Sal
G
G
Department of Biochemistry, Biophysics & Macromolecular Chemistry, University of Trieste, Italy.
Storici
P
P
Schneider
C
C
Romeo
D
D
Zanetti
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides; D001483:Base Sequence; D015152:Blotting, Northern; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics*; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009504:Neutrophils / Q000737:chemistry*; D015345:Oligonucleotide Probes; D010455:Peptides / Q000737:chemistry / Q000235:genetics*; D012333:RNA, Messenger / Q000032:analysis
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D015345:Oligonucleotide Probes; D010455:Peptides; D012333:RNA, Messenger; C073143:indolicidin; D004247:DNA