Purification, primary structures, and antibacterial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils

Michael E. Selsted, Yi Quan Tang, Wendy L. Morris, Patti A. McGuire, Michael J. Novotny, Wayne Smith, Agnes H. Henschen, James S Cullor

Research output: Contribution to journalArticle

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Abstract

A new family of cysteine-rich antimicrobial peptides from bovine neutrophils was isolated and characterized. Thirteen structurally homologous peptides were purified to homogeneity from a granule-rich cytoplasmic fraction of purified blood neutrophils. The complete sequences of the peptides were determined by a combination of enzymatic digestion, Edman degradation, and additional biochemical characterization of the carboxyl termini. The peptides are characterized by a highly cationic 38-42-residue chain which includes 6 invariantly spaced cysteines which form three disulfides. They share a highly conserved consensus sequence which is also found in a recently described epithelial antimicrobial peptide from bovine trachea. The in vitro antibacterial activities of the 13 neutrophil peptides, determined in assays using Staphylococcus aureus and Escherichia coli as test organisms, demonstrated that each peptide possessed antimicrobial activity, and that several were as active as the most potent neutrophil defensin, rabbit NP-1. Though the structural and functional attributes of the bovine neutrophil peptides are similar to those of defensins, the two peptide families are distinguished by their unique consensus sequences and additionally by differing tridisulfide motifs. We therefore propose that this new defensin-like antimicrobial peptide family be named β-defensins.

Original languageEnglish (US)
Pages (from-to)6641-6648
Number of pages8
JournalJournal of Biological Chemistry
Volume268
Issue number9
StatePublished - Mar 25 1993

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alpha-Defensins
Defensins
Purification
Peptides
Neutrophils
Consensus Sequence
Cysteine
Cytoplasmic Granules
Conserved Sequence
Trachea
Disulfides
Staphylococcus aureus
Digestion
Escherichia coli
Assays
Blood

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purification, primary structures, and antibacterial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils. / Selsted, Michael E.; Tang, Yi Quan; Morris, Wendy L.; McGuire, Patti A.; Novotny, Michael J.; Smith, Wayne; Henschen, Agnes H.; Cullor, James S.

In: Journal of Biological Chemistry, Vol. 268, No. 9, 25.03.1993, p. 6641-6648.

Research output: Contribution to journalArticle

Selsted, ME, Tang, YQ, Morris, WL, McGuire, PA, Novotny, MJ, Smith, W, Henschen, AH & Cullor, JS 1993, 'Purification, primary structures, and antibacterial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils', Journal of Biological Chemistry, vol. 268, no. 9, pp. 6641-6648.
Selsted, Michael E. ; Tang, Yi Quan ; Morris, Wendy L. ; McGuire, Patti A. ; Novotny, Michael J. ; Smith, Wayne ; Henschen, Agnes H. ; Cullor, James S. / Purification, primary structures, and antibacterial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils. In: Journal of Biological Chemistry. 1993 ; Vol. 268, No. 9. pp. 6641-6648.
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