Conference paper

Bovine Neutrophil Antibiotic Peptides and Their Precursors: Structure and Role in Innate Immunity

Domenico Romeo ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy
Renato Gennaro ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy
Margherita Zanetti ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy
Alessandro Tossi ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy
Barbara Skerlavaj ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy
Paola Storici ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy
Marco Scocchi ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy
Laura Litteri ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy
Donatella Verbanac ; Department of Biochemistry, Biopyhsics and Macromolecular Chemistry, University of Trieste and Department of Medical Sciences and Technology, University of Udine, Italy

Abstract

Four peptides were characterized in extracts of bovine neutrophil granules: an Arg-rich dodecapeptide, maintained in a cyclic structure by a disulfide bridge; a Trp-rich tridecapeptide named indo- licidin; and two 43- and 59 amino acids long peptides, named Bac5 and Bac7, with frequent repeats of the triplets Arg-Pro-Pro and Pro-Arg-Pro, respectively.
The full length cDNA of the first three of these peptides was characterized recently. Sequence analysis showed that the prosequences of the predicted precursors of all the three peptides are highly identical and exhibited also a remarkable similarity to cathelin, a porcine inhibitor of cathepsin L. Purified proBacö actually proved in in vitro assays to inhibit cathepsin L, but not other cysteine proteinases such as cathepsin B. Unlike proBacö, proBac7 is selectively chemotactic to monocytes.
Several fragments of Bac5 and Bac7 (from 6 to 35 residues) were synthesized by the Fmoc method. The results of antibacterial assays show that the N-terminal portion, the most cationic one in both Bac5 and Bac7, is essential for the antimicrobial activity and that the minimal length necessary to arrest the growth of susceptible bacteria is 18-20 residues.

Keywords

Hrčak ID:

136720

URI

https://hrcak.srce.hr/136720

Publication date:

1.9.1995.

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