Prophenin-1, an exceptionally proline-rich antimicrobial peptide from porcine leukocytes

FEBS Lett. 1995 Mar 27;362(1):65-9. doi: 10.1016/0014-5793(95)00210-z.

Abstract

We purified and characterized an unusual antimicrobial peptide, prophenin-1 (PF-1), from porcine leukocytes. The peptide had a mass of 8,683 and contained 79 residues, including 42 (53.2%) prolines and 15 (19.0%) phenylalanines. Its N-terminal 60 residues consisted of three perfect and three nearly perfect repeats of a decamer, FPPPNFPGPR. Prophenin-1 was encoded on a cathelin-containing precursor and showed substantially more activity against E. coli, a Gram-negative bacterium, than against Listeria monocytogenes, a Gram-positive organism, in vitro.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / isolation & purification
  • Anti-Bacterial Agents / pharmacology*
  • Antimicrobial Cationic Peptides
  • Escherichia coli / drug effects
  • Leukocytes / chemistry*
  • Listeria monocytogenes / drug effects
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Molecular Weight
  • Proteins / chemistry*
  • Proteins / isolation & purification
  • Proteins / pharmacology*
  • Swine / blood

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Proteins
  • prophenin 1