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Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss

Research output: Contribution to journalArticle

DOI

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Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss. / Fernandes, Jorge; Kemp, Graham Duncan; Molle, MG; Smith, Valerie Jane.

In: Biochemical Journal, Vol. 368, No. 2, 01.12.2002, p. 611-620.

Research output: Contribution to journalArticle

Harvard

Fernandes, J, Kemp, GD, Molle, MG & Smith, VJ 2002, 'Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss' Biochemical Journal, vol. 368, no. 2, pp. 611-620. https://doi.org/10.1042/BJ20020980

APA

Fernandes, J., Kemp, G. D., Molle, MG., & Smith, V. J. (2002). Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss. Biochemical Journal, 368(2), 611-620. https://doi.org/10.1042/BJ20020980

Vancouver

Fernandes J, Kemp GD, Molle MG, Smith VJ. Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss. Biochemical Journal. 2002 Dec 1;368(2):611-620. https://doi.org/10.1042/BJ20020980

Author

Fernandes, Jorge ; Kemp, Graham Duncan ; Molle, MG ; Smith, Valerie Jane. / Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss. In: Biochemical Journal. 2002 ; Vol. 368, No. 2. pp. 611-620.

Bibtex - Download

@article{03c6f1813c4c4bd39fb8490837d449e4,
title = "Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss",
abstract = "Skin exudates of rainbow trout contain a potent 13.6 kDa antimicrobial protein which, from partial internal amino acid sequencing, peptide mass fingerprinting, matrix-associated laser desorption/ionization MS and amino acid analysis, seems to be historic H2A, acetylated at the N-terminus. The protein, purified to homogeneity by ion-exchange and reversed-phase chromatography, exhibits powerful anti-bacterial activity against Grain-positive bacteria, with minimal inhibitory concentrations in the submicromolar range. Kinetic analysis revealed that at a concentration of 0.3 muM all test bacteria lose viability after 30 min incubation. Weaker activity is also displayed against the yeast Saccharomyces cerevisiae. The protein is salt-sensitive and has no haemolytic activity towards trout erythrocytes at concentrations below 0.3 muM. Reconstitution of the protein in a planar lipid bilayer strongly disturbs the membrane but does not form stable ion channels, indicating that its anti-bacterial activity is probably not due to pore-forming properties. This is the first report to show that, in addition to its classical function in the cell, histone H2A has extremely strong anti-microbial properties and could therefore help contribute to protection against bacterial invasion.",
keywords = "anti-bacterial protein, epithelium, mucosal immunity, nucleosome, PORE-FORMING PROPERTIES, ANTIMICROBIAL PEPTIDE, EPIDERMAL MUCUS, PROTEIN, FISH, EXPRESSION, FLOUNDER, SEQUENCE, MEMBRANE, PLEUROCIDIN",
author = "Jorge Fernandes and Kemp, {Graham Duncan} and MG Molle and Smith, {Valerie Jane}",
year = "2002",
month = "12",
day = "1",
doi = "10.1042/BJ20020980",
language = "English",
volume = "368",
pages = "611--620",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss

AU - Fernandes, Jorge

AU - Kemp, Graham Duncan

AU - Molle, MG

AU - Smith, Valerie Jane

PY - 2002/12/1

Y1 - 2002/12/1

N2 - Skin exudates of rainbow trout contain a potent 13.6 kDa antimicrobial protein which, from partial internal amino acid sequencing, peptide mass fingerprinting, matrix-associated laser desorption/ionization MS and amino acid analysis, seems to be historic H2A, acetylated at the N-terminus. The protein, purified to homogeneity by ion-exchange and reversed-phase chromatography, exhibits powerful anti-bacterial activity against Grain-positive bacteria, with minimal inhibitory concentrations in the submicromolar range. Kinetic analysis revealed that at a concentration of 0.3 muM all test bacteria lose viability after 30 min incubation. Weaker activity is also displayed against the yeast Saccharomyces cerevisiae. The protein is salt-sensitive and has no haemolytic activity towards trout erythrocytes at concentrations below 0.3 muM. Reconstitution of the protein in a planar lipid bilayer strongly disturbs the membrane but does not form stable ion channels, indicating that its anti-bacterial activity is probably not due to pore-forming properties. This is the first report to show that, in addition to its classical function in the cell, histone H2A has extremely strong anti-microbial properties and could therefore help contribute to protection against bacterial invasion.

AB - Skin exudates of rainbow trout contain a potent 13.6 kDa antimicrobial protein which, from partial internal amino acid sequencing, peptide mass fingerprinting, matrix-associated laser desorption/ionization MS and amino acid analysis, seems to be historic H2A, acetylated at the N-terminus. The protein, purified to homogeneity by ion-exchange and reversed-phase chromatography, exhibits powerful anti-bacterial activity against Grain-positive bacteria, with minimal inhibitory concentrations in the submicromolar range. Kinetic analysis revealed that at a concentration of 0.3 muM all test bacteria lose viability after 30 min incubation. Weaker activity is also displayed against the yeast Saccharomyces cerevisiae. The protein is salt-sensitive and has no haemolytic activity towards trout erythrocytes at concentrations below 0.3 muM. Reconstitution of the protein in a planar lipid bilayer strongly disturbs the membrane but does not form stable ion channels, indicating that its anti-bacterial activity is probably not due to pore-forming properties. This is the first report to show that, in addition to its classical function in the cell, histone H2A has extremely strong anti-microbial properties and could therefore help contribute to protection against bacterial invasion.

KW - anti-bacterial protein

KW - epithelium

KW - mucosal immunity

KW - nucleosome

KW - PORE-FORMING PROPERTIES

KW - ANTIMICROBIAL PEPTIDE

KW - EPIDERMAL MUCUS

KW - PROTEIN

KW - FISH

KW - EXPRESSION

KW - FLOUNDER

KW - SEQUENCE

KW - MEMBRANE

KW - PLEUROCIDIN

UR - http://www.scopus.com/inward/record.url?scp=2242429813&partnerID=8YFLogxK

UR - http://www.biochemj.org/bj/368/bj3680611.htm

U2 - 10.1042/BJ20020980

DO - 10.1042/BJ20020980

M3 - Article

VL - 368

SP - 611

EP - 620

JO - Biochemical Journal

T2 - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -

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ID: 306327