Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss

A 6.7 kDa antimicrobial peptide was isolated from trout skin secretions using acid extraction followed by cation-exchange chromatography, C-18, solid-phase extraction, and C-18 reversed-phase HPLC. The molecular mass of this peptide, which is tentatively named oncorhyncin III, is 6671 Da, as determi...

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Published in:Biochemical Journal
Main Authors: Fernandes, Jorge, Saint, N, Kemp, Graham Duncan, Smith, Valerie Jane
Format: Article in Journal/Newspaper
Language:English
Published: 2003
Subjects:
Online Access:https://risweb.st-andrews.ac.uk/portal/en/researchoutput/onchorhyncin-iii-a-potent-antimicrobial-peptide-derived-from-the-nonhistone-chromosomal-protein-h6-of-rainbow-trout-oncorhynchus-mykiss(43355219-b6fc-4d1d-b319-8b0d64493abc).html
https://doi.org/10.1042/BJ20030259
http://www.scopus.com/inward/record.url?scp=0041364483&partnerID=8YFLogxK
id ftunstandrewcris:oai:risweb.st-andrews.ac.uk:publications/43355219-b6fc-4d1d-b319-8b0d64493abc
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spelling ftunstandrewcris:oai:risweb.st-andrews.ac.uk:publications/43355219-b6fc-4d1d-b319-8b0d64493abc 2023-05-15T15:32:42+02:00 Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss Fernandes, Jorge Saint, N Kemp, Graham Duncan Smith, Valerie Jane 2003-07-15 https://risweb.st-andrews.ac.uk/portal/en/researchoutput/onchorhyncin-iii-a-potent-antimicrobial-peptide-derived-from-the-nonhistone-chromosomal-protein-h6-of-rainbow-trout-oncorhynchus-mykiss(43355219-b6fc-4d1d-b319-8b0d64493abc).html https://doi.org/10.1042/BJ20030259 http://www.scopus.com/inward/record.url?scp=0041364483&partnerID=8YFLogxK eng eng info:eu-repo/semantics/restrictedAccess Fernandes , J , Saint , N , Kemp , G D & Smith , V J 2003 , ' Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss ' , Biochemical Journal , vol. 373 , no. 2 , pp. 621-628 . https://doi.org/10.1042/BJ20030259 antimicrobial peptide historic mucosal immunity oncorhyncin III teleost trout HUMAN CDNA SEQUENCE HISTONE H2A MULTIGENE FAMILY SKIN SECRETIONS ATLANTIC SALMON MECHANISM MEMBRANE BINDING HMG-14 TESTIS article 2003 ftunstandrewcris https://doi.org/10.1042/BJ20030259 2021-12-26T14:12:56Z A 6.7 kDa antimicrobial peptide was isolated from trout skin secretions using acid extraction followed by cation-exchange chromatography, C-18, solid-phase extraction, and C-18 reversed-phase HPLC. The molecular mass of this peptide, which is tentatively named oncorhyncin III, is 6671 Da, as determined by matrix-assisted laser-desorption ionization MS. N-terminal amino acid sequencing revealed that the first 13 residues of oncorhyncin III are identical with those of the non-histone chromosomal protein H6 from rainbow trout. Hence these data combined with the MS results indicate that oncorhyncin III is likely to be a cleavage product of the non-histone chromosomal protein H6 (residues 1-66) and that it probably contains two methylated residues or one double methylation. The purified peptide exhibits potent antibacterial activity against both Gram-positive and Gram-negative bacteria, with minimal inhibitory concentrations in the submicromolar range. The peptide is sensitive to NaCl, and displays no haemolytic activity towards trout erythrocytes at concentrations below 1 muM. Scanning electron microscopy revealed that oncorhyncin III does not cause direct disruption of bacterial cells. Reconstitution of the peptide in planar lipid bilayers strongly disturbs the membranes, but does not induce the formation of stable ion channels. Taken together, these results support the hypothesis that oncorhyncin III plays a role in mucosal innate host defence. Article in Journal/Newspaper Atlantic salmon University of St Andrews: Research Portal Biochemical Journal 373 2 621 628
institution Open Polar
collection University of St Andrews: Research Portal
op_collection_id ftunstandrewcris
language English
topic antimicrobial peptide
historic
mucosal immunity
oncorhyncin III
teleost
trout
HUMAN CDNA SEQUENCE
HISTONE H2A
MULTIGENE FAMILY
SKIN SECRETIONS
ATLANTIC SALMON
MECHANISM
MEMBRANE
BINDING
HMG-14
TESTIS
spellingShingle antimicrobial peptide
historic
mucosal immunity
oncorhyncin III
teleost
trout
HUMAN CDNA SEQUENCE
HISTONE H2A
MULTIGENE FAMILY
SKIN SECRETIONS
ATLANTIC SALMON
MECHANISM
MEMBRANE
BINDING
HMG-14
TESTIS
Fernandes, Jorge
Saint, N
Kemp, Graham Duncan
Smith, Valerie Jane
Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss
topic_facet antimicrobial peptide
historic
mucosal immunity
oncorhyncin III
teleost
trout
HUMAN CDNA SEQUENCE
HISTONE H2A
MULTIGENE FAMILY
SKIN SECRETIONS
ATLANTIC SALMON
MECHANISM
MEMBRANE
BINDING
HMG-14
TESTIS
description A 6.7 kDa antimicrobial peptide was isolated from trout skin secretions using acid extraction followed by cation-exchange chromatography, C-18, solid-phase extraction, and C-18 reversed-phase HPLC. The molecular mass of this peptide, which is tentatively named oncorhyncin III, is 6671 Da, as determined by matrix-assisted laser-desorption ionization MS. N-terminal amino acid sequencing revealed that the first 13 residues of oncorhyncin III are identical with those of the non-histone chromosomal protein H6 from rainbow trout. Hence these data combined with the MS results indicate that oncorhyncin III is likely to be a cleavage product of the non-histone chromosomal protein H6 (residues 1-66) and that it probably contains two methylated residues or one double methylation. The purified peptide exhibits potent antibacterial activity against both Gram-positive and Gram-negative bacteria, with minimal inhibitory concentrations in the submicromolar range. The peptide is sensitive to NaCl, and displays no haemolytic activity towards trout erythrocytes at concentrations below 1 muM. Scanning electron microscopy revealed that oncorhyncin III does not cause direct disruption of bacterial cells. Reconstitution of the peptide in planar lipid bilayers strongly disturbs the membranes, but does not induce the formation of stable ion channels. Taken together, these results support the hypothesis that oncorhyncin III plays a role in mucosal innate host defence.
format Article in Journal/Newspaper
author Fernandes, Jorge
Saint, N
Kemp, Graham Duncan
Smith, Valerie Jane
author_facet Fernandes, Jorge
Saint, N
Kemp, Graham Duncan
Smith, Valerie Jane
author_sort Fernandes, Jorge
title Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss
title_short Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss
title_full Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss
title_fullStr Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss
title_full_unstemmed Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss
title_sort onchorhyncin iii: a potent antimicrobial peptide derived from the non-histone chromosomal protein h6 of rainbow trout, oncorhynchus mykiss
publishDate 2003
url https://risweb.st-andrews.ac.uk/portal/en/researchoutput/onchorhyncin-iii-a-potent-antimicrobial-peptide-derived-from-the-nonhistone-chromosomal-protein-h6-of-rainbow-trout-oncorhynchus-mykiss(43355219-b6fc-4d1d-b319-8b0d64493abc).html
https://doi.org/10.1042/BJ20030259
http://www.scopus.com/inward/record.url?scp=0041364483&partnerID=8YFLogxK
genre Atlantic salmon
genre_facet Atlantic salmon
op_source Fernandes , J , Saint , N , Kemp , G D & Smith , V J 2003 , ' Onchorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss ' , Biochemical Journal , vol. 373 , no. 2 , pp. 621-628 . https://doi.org/10.1042/BJ20030259
op_rights info:eu-repo/semantics/restrictedAccess
op_doi https://doi.org/10.1042/BJ20030259
container_title Biochemical Journal
container_volume 373
container_issue 2
container_start_page 621
op_container_end_page 628
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