Proline Conformation-Dependent Antimicrobial Activity of a Proline-Rich Histone H1 N-Terminal Peptide Fragment Isolated from the Skin Mucus of Atlantic Salmon
A 30-residue N-terminally acetylated peptide derived from the N-terminal part of histone H1 was identified as the dominant antimicrobial peptide in skin mucus from Atlantic salmon (Salmo salar). The peptide (termed salmon antimicrobial peptide [SAMP H1]) was purified to homogeneity by a combination...
Published in: | Antimicrobial Agents and Chemotherapy |
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ftpubmed:oai:pubmedcentral.nih.gov:1140541 2023-05-15T15:31:52+02:00 Proline Conformation-Dependent Antimicrobial Activity of a Proline-Rich Histone H1 N-Terminal Peptide Fragment Isolated from the Skin Mucus of Atlantic Salmon Lüders, Torben Birkemo, Gunn Alice Nissen-Meyer, Jon Andersen, Øivind Nes, Ingolf F. 2005-06 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1140541 http://www.ncbi.nlm.nih.gov/pubmed/15917539 https://doi.org/10.1128/AAC.49.6.2399-2406.2005 en eng American Society for Microbiology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1140541 http://www.ncbi.nlm.nih.gov/pubmed/15917539 http://dx.doi.org/10.1128/AAC.49.6.2399-2406.2005 Copyright © 2005, American Society for Microbiology Mechanisms of Action: Physiological Effects Text 2005 ftpubmed https://doi.org/10.1128/AAC.49.6.2399-2406.2005 2013-08-30T10:15:46Z A 30-residue N-terminally acetylated peptide derived from the N-terminal part of histone H1 was identified as the dominant antimicrobial peptide in skin mucus from Atlantic salmon (Salmo salar). The peptide (termed salmon antimicrobial peptide [SAMP H1]) was purified to homogeneity by a combination of reversed-phase and cation-exchange chromatographies. By Edman degradation of the deacetylated peptide and by sequencing of the PCR-amplified DNA that encodes the peptide, the complete amino acid sequence was determined to be AEVAPAPAAAAPAKAPKKKAAAKPKKAGPS. The theoretical molecular weight of N-terminally acetylated SAMP H1 was calculated to be 2,836, which is the same as that determined by matrix-assisted laser desorption ionization mass spectrometry. The peptide was active against both gram-negative and -positive bacteria. The N-terminal acetyl group was not necessary for activity since deacetylation did not reduce the activity. A synthetic peptide whose sequence was identical to that of the isolated fragment was initially inactive but could be activated by binding it to a cation-exchange column. Treatment of the synthetic peptide when it was bound to the exchange column with peptidylproline cis-trans-isomerase increased the amount of active peptide, indicating that isomerization of the proline peptide bond(s) was necessary for activation of the synthetic peptide. Comparison of the active and inactive forms by circular dichroism and chromatographic analyses suggests that the active form, both the natural and the synthetic forms, is more structured, condensed, and rigid than the inactive form, which has a more nonstructured conformation. This work shows for the first time the importance of proline isomers in the activity of an antimicrobial peptide. Text Atlantic salmon Salmo salar PubMed Central (PMC) Antimicrobial Agents and Chemotherapy 49 6 2399 2406 |
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English |
topic |
Mechanisms of Action: Physiological Effects |
spellingShingle |
Mechanisms of Action: Physiological Effects Lüders, Torben Birkemo, Gunn Alice Nissen-Meyer, Jon Andersen, Øivind Nes, Ingolf F. Proline Conformation-Dependent Antimicrobial Activity of a Proline-Rich Histone H1 N-Terminal Peptide Fragment Isolated from the Skin Mucus of Atlantic Salmon |
topic_facet |
Mechanisms of Action: Physiological Effects |
description |
A 30-residue N-terminally acetylated peptide derived from the N-terminal part of histone H1 was identified as the dominant antimicrobial peptide in skin mucus from Atlantic salmon (Salmo salar). The peptide (termed salmon antimicrobial peptide [SAMP H1]) was purified to homogeneity by a combination of reversed-phase and cation-exchange chromatographies. By Edman degradation of the deacetylated peptide and by sequencing of the PCR-amplified DNA that encodes the peptide, the complete amino acid sequence was determined to be AEVAPAPAAAAPAKAPKKKAAAKPKKAGPS. The theoretical molecular weight of N-terminally acetylated SAMP H1 was calculated to be 2,836, which is the same as that determined by matrix-assisted laser desorption ionization mass spectrometry. The peptide was active against both gram-negative and -positive bacteria. The N-terminal acetyl group was not necessary for activity since deacetylation did not reduce the activity. A synthetic peptide whose sequence was identical to that of the isolated fragment was initially inactive but could be activated by binding it to a cation-exchange column. Treatment of the synthetic peptide when it was bound to the exchange column with peptidylproline cis-trans-isomerase increased the amount of active peptide, indicating that isomerization of the proline peptide bond(s) was necessary for activation of the synthetic peptide. Comparison of the active and inactive forms by circular dichroism and chromatographic analyses suggests that the active form, both the natural and the synthetic forms, is more structured, condensed, and rigid than the inactive form, which has a more nonstructured conformation. This work shows for the first time the importance of proline isomers in the activity of an antimicrobial peptide. |
format |
Text |
author |
Lüders, Torben Birkemo, Gunn Alice Nissen-Meyer, Jon Andersen, Øivind Nes, Ingolf F. |
author_facet |
Lüders, Torben Birkemo, Gunn Alice Nissen-Meyer, Jon Andersen, Øivind Nes, Ingolf F. |
author_sort |
Lüders, Torben |
title |
Proline Conformation-Dependent Antimicrobial Activity of a Proline-Rich Histone H1 N-Terminal Peptide Fragment Isolated from the Skin Mucus of Atlantic Salmon |
title_short |
Proline Conformation-Dependent Antimicrobial Activity of a Proline-Rich Histone H1 N-Terminal Peptide Fragment Isolated from the Skin Mucus of Atlantic Salmon |
title_full |
Proline Conformation-Dependent Antimicrobial Activity of a Proline-Rich Histone H1 N-Terminal Peptide Fragment Isolated from the Skin Mucus of Atlantic Salmon |
title_fullStr |
Proline Conformation-Dependent Antimicrobial Activity of a Proline-Rich Histone H1 N-Terminal Peptide Fragment Isolated from the Skin Mucus of Atlantic Salmon |
title_full_unstemmed |
Proline Conformation-Dependent Antimicrobial Activity of a Proline-Rich Histone H1 N-Terminal Peptide Fragment Isolated from the Skin Mucus of Atlantic Salmon |
title_sort |
proline conformation-dependent antimicrobial activity of a proline-rich histone h1 n-terminal peptide fragment isolated from the skin mucus of atlantic salmon |
publisher |
American Society for Microbiology |
publishDate |
2005 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1140541 http://www.ncbi.nlm.nih.gov/pubmed/15917539 https://doi.org/10.1128/AAC.49.6.2399-2406.2005 |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1140541 http://www.ncbi.nlm.nih.gov/pubmed/15917539 http://dx.doi.org/10.1128/AAC.49.6.2399-2406.2005 |
op_rights |
Copyright © 2005, American Society for Microbiology |
op_doi |
https://doi.org/10.1128/AAC.49.6.2399-2406.2005 |
container_title |
Antimicrobial Agents and Chemotherapy |
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49 |
container_issue |
6 |
container_start_page |
2399 |
op_container_end_page |
2406 |
_version_ |
1766362371598581760 |