Cellular and Molecular Life Sciences CMLS

, Volume 54, Issue 5, pp 467–475

Antimicrobial activity in the skin of the channel catfish Ictalurus punctatus: characterization of broad-spectrum histone-like antimicrobial proteins

  • D. Robinette
  • S. Wada
  • T. Arroll
  • M. G. Levy
  • W. L. Miller
  • E. J. Noga

DOI: 10.1007/s000180050175

Cite this article as:
Robinette, D., Wada, S., Arroll, T. et al. CMLS, Cell. Mol. Life Sci. (1998) 54: 467. doi:10.1007/s000180050175

Abstract.

Three antibacterial proteins were isolated from acid extracts of channel catfish (Ictalurus punctatus) skin by cation exchange chromatography and reverse-phase high-pressure liquid chromatography. The molecular masses of the proteins were 15.5, 15.5 and 30 kD as determined by SDS-polyacrylamide gel electrophoresis. Mass spectrometry, amino acid composition and amino acid sequence data suggest that the most abundant protein is closely related to histone H2B. The H2B-like protein was inhibitory to Aeromonas hydrophila and Saprolegnia spp., which are important bacterial and fungal pathogens of fish. These findings suggest that histones may be important defensive molecules in fish.

Key words. Antimicrobial proteins; catfish; non-specific immunity; histones. 

Copyright information

© Birkhäuser Verlag Basel, 1998

Authors and Affiliations

  • D. Robinette
    • 1
  • S. Wada
    • 1
  • T. Arroll
    • 1
  • M. G. Levy
    • 2
  • W. L. Miller
    • 3
  • E. J. Noga
    • 1
  1. 1.Department of Companion Animal and Special Species Medicine, College of Veterinary Medicine, North Carolina State University, Raleigh (North Carolina 27606, USA), Fax +1 919 829 4336, e-mail: ed_noga@ncsu.eduUS
  2. 2.Department of Microbiology, Pathology and Parasitology, College of Veterinary Medicine, North Carolina State University, Raleigh (North Carolina 27606, USA)US
  3. 3.Department of Biochemistry, North Carolina State University, Raleigh (North Carolina 27695, USA)US

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