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A characterization of antimicrobial ...

Robinette, David Wiley, Jr.

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A characterization of antimicrobial activity associated with histone-like proteins in the skin of the channel catfish, Ictalurus punctatus Rafinesque.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	A characterization of antimicrobial activity associated with histone-like proteins in the skin of the channel catfish, Ictalurus punctatus Rafinesque./
Author:	Robinette, David Wiley, Jr.
Description:	104 p.
Notes:	Co-Chairs: Edward J. Noga; Michael G. Levy.
Contained By:	Dissertation Abstracts International60-03B.
Subject:	Agriculture, Animal Pathology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9922703
ISBN:	9780599222694

A characterization of antimicrobial activity associated with histone-like proteins in the skin of the channel catfish, Ictalurus punctatus Rafinesque.
Robinette, David Wiley, Jr.

A characterization of antimicrobial activity associated with histone-like proteins in the skin of the channel catfish, Ictalurus punctatus Rafinesque. - 104 p.

Co-Chairs: Edward J. Noga; Michael G. Levy.

Thesis (Ph.D.)--North Carolina State University, 1998.

Three antibacterial proteins were isolated from acid extracts of channel catfish (Ictalurus punctatus) skin by a combination of cation exchange chromatography and reverse-phase high pressure liquid chromatography (RP-HPLC). 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 partial N-terminal amino acid sequence data suggest that the most abundant protein is closely related to histone H2B. Amino acid composition data for the second most abundant antibacterial protein was consistent with that of histone H1, while mass spectrometry and partial N-terminal amino acid sequence indicated that the least abundant protein was also closely related to histone H2B. Due to their similarity to histones, the catfish antibacterial proteins were designated histone-like proteins (HLP) 1, 2, and 3 in decreasing order of predominance. HLP-1 demonstrated broad-spectrum antimicrobial activity, and was inhibitory to several isolates of Aeromonas hydrophila as well as Vibrio alginolyticus, which are important bacterial pathogens of fish. Both HLP-1 and 2 were cidal to E. coli D31, and the lethal concentration of HLP-1 against E. coli D31 was comparable to the cecropin insect defense peptides. Collectively, these findings suggest that histones or histone-like molecules may be important components of non-specific antimicrobial defenses in catfish.

ISBN: 9780599222694Subjects--Topical Terms:

1021764
Agriculture, Animal Pathology.

A characterization of antimicrobial activity associated with histone-like proteins in the skin of the channel catfish, Ictalurus punctatus Rafinesque.
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100 1 $a Robinette, David Wiley, Jr. $3 1269130
245 1 2 $a A characterization of antimicrobial activity associated with histone-like proteins in the skin of the channel catfish, Ictalurus punctatus Rafinesque.
300 $a 104 p.
500 $a Co-Chairs: Edward J. Noga; Michael G. Levy.
500 $a Source: Dissertation Abstracts International, Volume: 60-03, Section: B, page: 0889.
502 $a Thesis (Ph.D.)--North Carolina State University, 1998.
520 $a Three antibacterial proteins were isolated from acid extracts of channel catfish (Ictalurus punctatus) skin by a combination of cation exchange chromatography and reverse-phase high pressure liquid chromatography (RP-HPLC). 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 partial N-terminal amino acid sequence data suggest that the most abundant protein is closely related to histone H2B. Amino acid composition data for the second most abundant antibacterial protein was consistent with that of histone H1, while mass spectrometry and partial N-terminal amino acid sequence indicated that the least abundant protein was also closely related to histone H2B. Due to their similarity to histones, the catfish antibacterial proteins were designated histone-like proteins (HLP) 1, 2, and 3 in decreasing order of predominance. HLP-1 demonstrated broad-spectrum antimicrobial activity, and was inhibitory to several isolates of Aeromonas hydrophila as well as Vibrio alginolyticus, which are important bacterial pathogens of fish. Both HLP-1 and 2 were cidal to E. coli D31, and the lethal concentration of HLP-1 against E. coli D31 was comparable to the cecropin insect defense peptides. Collectively, these findings suggest that histones or histone-like molecules may be important components of non-specific antimicrobial defenses in catfish.
520 $a In laboratory experiments, stress associated with chronic crowding confinement and poor water quality resulted in a significant increase in antibacterial activity in skin extracts of fish confined for 1 week; antibacterial activity of fish confined for 3 weeks was similar to unstressed controls, and was significantly depressed in fish confined for 4 weeks. An Enzyme-linked Immunosorbent Assay (ELISA) utilizing anti-histone H2B antibodies was used to examine the effect of chronic confinement on skin HLP levels. ELISA results indicated that HLP levels were significantly depressed in fish confined for 1 week or longer. Analysis of antibacterial activity, protein concentration, and RP-HPLC of HLP semi-purified by cation exchange chromatography on CM sep pak cartridges suggested that total levels of HLP were depressed in chronically confined fish compared to controls, supporting ELISA observations. The increase in antibacterial activity in skin extracts of fish confined for 1 week could not be explained by an increase in HLP-associated activity, and suggested the possibility of induction of non-HLP factor(s) which may enhance antibacterial defenses in the skin as an adaptation to stress. These results provide new information which may contribute to a better understanding of the effects of stress on non-specific immunity in fish, and may be useful in future studies to develop methods for enhancing disease resistance in aquaculture species.
590 $a School code: 0155.
650 4 $a Agriculture, Animal Pathology. $3 1021764
650 4 $a Agriculture, Fisheries and Aquaculture. $3 1020913
650 4 $a Biology, Animal Physiology. $3 1017835
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Health Sciences, Immunology. $3 1017716
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710 2 $a North Carolina State University. $3 1018772
773 0 $t Dissertation Abstracts International $g 60-03B.
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790 1 0 $a Levy, Michael G., $e advisor
790 1 0 $a Noga, Edward J., $e advisor
791 $a Ph.D.
792 $a 1998
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9922703