cDNA sequence analysis of an antibiotic dodecapeptide from neutrophils.
The full-length cDNA of a neutrophil antibiotic dodecapeptide has been cloned by reverse transcription/PCR from bovine bone marrow RNA. This peptide was originally isolated from bovine neutrophils, and shown to exert a potent antimicrobial activity in vitro on both Escherichia coli and Staphylococcus aureus. The cDNA codes for a polypeptide of 155 amino acid residues with a predicted mass of 17,629 Da and a pI of 8.03. The deduced sequence comprises a putative signal peptide of 29 amino acids, a 114 residue pro-region, and a carboxy-terminal dodecapeptide corresponding to the mature antibiotic. The pro-sequence displays extensive identity to corresponding regions of other structurally unrelated antibiotic peptides of bovine neutrophils recently cloned.
Storici
P
P
Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Italy.
Del Sal
G
G
Schneider
C
C
Zanetti
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents; D001483:Base Sequence; D001853:Bone Marrow; D002417:Cattle; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000737:chemistry*; D009842:Oligopeptides / Q000096:biosynthesis / Q000235:genetics*; D010456:Peptides, Cyclic / Q000096:biosynthesis / Q000235:genetics*; D011498:Protein Precursors / Q000096:biosynthesis / Q000235:genetics*; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D000900:Anti-Bacterial Agents; D009842:Oligopeptides; D010456:Peptides, Cyclic; D011498:Protein Precursors