Antimicrobial activity in the skin of the channel catfish Ictalurus punctatus: characterization of broad-spectrum histone-like antimicrobial proteins.
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.
Robinette
D
D
Department of Companion Animal and Special Species Medicine, College of Veterinary Medicine, North Carolina State University, Raleigh 27606, USA.
Wada
S
S
Arroll
T
T
Levy
M G
MG
Miller
W L
WL
Noga
E J
EJ
D000333:Aeromonas / Q000187:drug effects; D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000302:isolation & purification* / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005393:Fish Diseases / Q000276:immunology; D006657:Histones / Q000737:chemistry*; D007059:Ictaluridae / Q000276:immunology*; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009868:Oomycetes / Q000187:drug effects; D011506:Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D012867:Skin / Q000737:chemistry* / Q000382:microbiology
D000900:Anti-Bacterial Agents; D006657:Histones; D011506:Proteins