ub.xmlui.mirage2.page-structure.muninLogoub.xmlui.mirage2.page-structure.openResearchArchiveLogo
    • EnglishEnglish
    • norsknorsk
  • Velg spraaknorsk 
    • EnglishEnglish
    • norsknorsk
  • Administrasjon/UB
Vis innførsel 
  •   Hjem
  • Fakultet for biovitenskap, fiskeri og økonomi
  • Norges fiskerihøgskole
  • Artikler, rapporter og annet (Norges fiskerihøgskole)
  • Vis innførsel
  •   Hjem
  • Fakultet for biovitenskap, fiskeri og økonomi
  • Norges fiskerihøgskole
  • Artikler, rapporter og annet (Norges fiskerihøgskole)
  • Vis innførsel
JavaScript is disabled for your browser. Some features of this site may not work without it.

Novel antimicrobial peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible sea urchin Echinus esculentus have 6-br-trp post-translational modifications

Permanent lenke
https://hdl.handle.net/10037/10268
DOI
https://doi.org/10.1371/journal.pone.0151820
Thumbnail
Åpne
article.pdf (3.142Mb)
(PDF)
Dato
2016-03-23
Type
Journal article
Tidsskriftartikkel
Peer reviewed

Forfatter
Solstad, Runar Gjerp; Li, Chun; Isaksson, Johan; Johansen, Jostein a; Svenson, Johan; Stensvåg, Klara; Haug, Tor
Sammendrag
The global problem of microbial resistance to antibiotics has resulted in an urgent need to develop new antimicrobial agents. Natural antimicrobial peptides are considered promising candidates for drug development. Echinoderms, which rely on innate immunity factors in the defence against harmful microorganisms, are sources of novel antimicrobial peptides. This study aimed to isolate and characterise antimicrobial peptides from the Edible sea urchin Echinus esculentus. Using bioassay-guided purification and cDNA cloning, three antimicrobial peptides were characterised from the haemocytes of the sea urchin; two heterodimeric peptides and a cysteine-rich peptide. The peptides were named EeCentrocin 1 and 2 and EeStrongylocin 2, respectively, due to their apparent homology to the published centrocins and strongylocins isolated from the green sea urchin Strongylocentrotus droebachiensis. The two centrocin-like peptides EeCentrocin 1 and 2 are intramolecularly connected via a disulphide bond to form a heterodimeric structure, containing a cationic heavy chain of 30 and 32 amino acids and a light chain of 13 amino acids. Additionally, the light chain of EeCentrocin 2 seems to be N-terminally blocked by a pyroglutamic acid residue. The heavy chains of EeCentrocins 1 and 2 were synthesised and shown to be responsible for the antimicrobial activity of the natural peptides. EeStrongylocin 2 contains 6 cysteines engaged in 3 disulphide bonds. A fourth peptide (Ee4635) was also discovered but not fully characterised. Using mass spectrometric and NMR analyses, EeCentrocins 1 and 2, EeStrongylocin 2 and Ee4635 were all shown to contain post-translationally brominated Trp residues in the 6 position of the indole ring.
Beskrivelse
This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
This article is also available via DOI:10.1371/journal.pone.0151820
Forlag
Public Library of Science
Sitering
Solstad RG, Li C, Isaksson JM, Johansen Ja, Svenson J, Stensvåg K, Haug T. Novel antimicrobial peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible sea urchin Echinus esculentus have 6-br-trp post-translational modifications. PLoS ONE. 2016;11(3)
Metadata
Vis full innførsel
Samlinger
  • Artikler, rapporter og annet (kjemi) [565]
  • Artikler, rapporter og annet (Norges fiskerihøgskole) [1053]

Bla

Bla i hele MuninEnheter og samlingerForfatterlisteTittelDatoBla i denne samlingenForfatterlisteTittelDato
Logg inn

Statistikk

Antall visninger
UiT

Munin bygger på DSpace

UiT Norges Arktiske Universitet
Universitetsbiblioteket
uit.no/ub - munin@ub.uit.no

Tilgjengelighetserklæring