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{{Seed}}
[[Image:1zfu.png|left|200px]]


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==Plectasin:A peptide antibiotic with therapeutic potential from a saprophytic fungus==
The line below this paragraph, containing "STRUCTURE_1zfu", creates the "Structure Box" on the page.
<StructureSection load='1zfu' size='340' side='right'caption='[[1zfu]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1zfu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoplectania_nigrella Pseudoplectania nigrella]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZFU FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zfu OCA], [https://pdbe.org/1zfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zfu RCSB], [https://www.ebi.ac.uk/pdbsum/1zfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zfu ProSAT]</span></td></tr>
{{STRUCTURE_1zfu|  PDB=1zfu  |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/DEFPL_PSENR DEFPL_PSENR] Antimicrobial peptide that potently acts against several species of Gram-positive bacteria (PubMed:16222292, PubMed:19472324). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20508130). It does not disrupt cell membranes (PubMed:20508130). Is especially active against numerous clinical isolates of S.pneumoniae, including all 90 different serotypes and isolates resistant to clinically used antibiotics (PubMed:16222292). In vitro, shows considerable selectivity for bacteria over mammalian cells (PubMed:16222292). The peptide synthesized in D-amino acids does not show antibacterial activity (PubMed:19472324). In vitro, acts on voltage-gated potassium channels by moderately inhibiting mammalian Kv1.3/KCNA3 (IC(50)=2.8 uM), and moderately inhibiting others potassium channels (PubMed:25568977).<ref>PMID:16222292</ref> <ref>PMID:25568977</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Animals and higher plants express endogenous peptide antibiotics called defensins. These small cysteine-rich peptides are active against bacteria, fungi and viruses. Here we describe plectasin-the first defensin to be isolated from a fungus, the saprophytic ascomycete Pseudoplectania nigrella. Plectasin has primary, secondary and tertiary structures that closely resemble those of defensins found in spiders, scorpions, dragonflies and mussels. Recombinant plectasin was produced at a very high, and commercially viable, yield and purity. In vitro, the recombinant peptide was especially active against Streptococcus pneumoniae, including strains resistant to conventional antibiotics. Plectasin showed extremely low toxicity in mice, and cured them of experimental peritonitis and pneumonia caused by S. pneumoniae as efficaciously as vancomycin and penicillin. These findings identify fungi as a novel source of antimicrobial defensins, and show the therapeutic potential of plectasin. They also suggest that the defensins of insects, molluscs and fungi arose from a common ancestral gene.


===Plectasin:A peptide antibiotic with therapeutic potential from a saprophytic fungus===
Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus.,Mygind PH, Fischer RL, Schnorr KM, Hansen MT, Sonksen CP, Ludvigsen S, Raventos D, Buskov S, Christensen B, De Maria L, Taboureau O, Yaver D, Elvig-Jorgensen SG, Sorensen MV, Christensen BE, Kjaerulff S, Frimodt-Moller N, Lehrer RI, Zasloff M, Kristensen HH Nature. 2005 Oct 13;437(7061):975-80. PMID:16222292<ref>PMID:16222292</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_16222292}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1zfu" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 16222292 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_16222292}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1ZFU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudoplectania_nigrella Pseudoplectania nigrella]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZFU OCA].
 
==Reference==
Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus., Mygind PH, Fischer RL, Schnorr KM, Hansen MT, Sonksen CP, Ludvigsen S, Raventos D, Buskov S, Christensen B, De Maria L, Taboureau O, Yaver D, Elvig-Jorgensen SG, Sorensen MV, Christensen BE, Kjaerulff S, Frimodt-Moller N, Lehrer RI, Zasloff M, Kristensen HH, Nature. 2005 Oct 13;437(7061):975-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16222292 16222292]
[[Category: Pseudoplectania nigrella]]
[[Category: Pseudoplectania nigrella]]
[[Category: Single protein]]
[[Category: Buskov S]]
[[Category: Buskov, S.]]
[[Category: Christensen B]]
[[Category: Christensen, B.]]
[[Category: Christensen BE]]
[[Category: Christensen, B E.]]
[[Category: De Maria L]]
[[Category: Elvig-Jorgensen, S G.]]
[[Category: Elvig-Jorgensen SG]]
[[Category: Fischer, R L.]]
[[Category: Fischer RL]]
[[Category: Frimodt-Moller, N.]]
[[Category: Frimodt-Moller N]]
[[Category: Hansen, M T.]]
[[Category: Hansen MT]]
[[Category: Kjaerulf, S.]]
[[Category: Kjaerulf S]]
[[Category: Kristensen, H H.]]
[[Category: Kristensen HH]]
[[Category: Lehrer, R I.]]
[[Category: Lehrer RI]]
[[Category: Ludvigsen, S.]]
[[Category: Ludvigsen S]]
[[Category: Maria, L De.]]
[[Category: Mygind PH]]
[[Category: Mygind, P H.]]
[[Category: Raventos D]]
[[Category: Raventos, D.]]
[[Category: Schnorr K]]
[[Category: Schnorr, K.]]
[[Category: Sonksen CP]]
[[Category: Sonksen, C P.]]
[[Category: Sorensen MV]]
[[Category: Sorensen, M V.]]
[[Category: Taboureau O]]
[[Category: Taboureau, O.]]
[[Category: Yaver D]]
[[Category: Yaver, D.]]
[[Category: Zasloff M]]
[[Category: Zasloff, M.]]
[[Category: Defensin,antimicrobial peptide,cysteine stabilized alpha-beta motif]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:32:31 2008''

Latest revision as of 10:45, 30 October 2024

Plectasin:A peptide antibiotic with therapeutic potential from a saprophytic fungusPlectasin:A peptide antibiotic with therapeutic potential from a saprophytic fungus

Structural highlights

1zfu is a 1 chain structure with sequence from Pseudoplectania nigrella. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 10 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DEFPL_PSENR Antimicrobial peptide that potently acts against several species of Gram-positive bacteria (PubMed:16222292, PubMed:19472324). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20508130). It does not disrupt cell membranes (PubMed:20508130). Is especially active against numerous clinical isolates of S.pneumoniae, including all 90 different serotypes and isolates resistant to clinically used antibiotics (PubMed:16222292). In vitro, shows considerable selectivity for bacteria over mammalian cells (PubMed:16222292). The peptide synthesized in D-amino acids does not show antibacterial activity (PubMed:19472324). In vitro, acts on voltage-gated potassium channels by moderately inhibiting mammalian Kv1.3/KCNA3 (IC(50)=2.8 uM), and moderately inhibiting others potassium channels (PubMed:25568977).[1] [2]

Publication Abstract from PubMed

Animals and higher plants express endogenous peptide antibiotics called defensins. These small cysteine-rich peptides are active against bacteria, fungi and viruses. Here we describe plectasin-the first defensin to be isolated from a fungus, the saprophytic ascomycete Pseudoplectania nigrella. Plectasin has primary, secondary and tertiary structures that closely resemble those of defensins found in spiders, scorpions, dragonflies and mussels. Recombinant plectasin was produced at a very high, and commercially viable, yield and purity. In vitro, the recombinant peptide was especially active against Streptococcus pneumoniae, including strains resistant to conventional antibiotics. Plectasin showed extremely low toxicity in mice, and cured them of experimental peritonitis and pneumonia caused by S. pneumoniae as efficaciously as vancomycin and penicillin. These findings identify fungi as a novel source of antimicrobial defensins, and show the therapeutic potential of plectasin. They also suggest that the defensins of insects, molluscs and fungi arose from a common ancestral gene.

Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus.,Mygind PH, Fischer RL, Schnorr KM, Hansen MT, Sonksen CP, Ludvigsen S, Raventos D, Buskov S, Christensen B, De Maria L, Taboureau O, Yaver D, Elvig-Jorgensen SG, Sorensen MV, Christensen BE, Kjaerulff S, Frimodt-Moller N, Lehrer RI, Zasloff M, Kristensen HH Nature. 2005 Oct 13;437(7061):975-80. PMID:16222292[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Mygind PH, Fischer RL, Schnorr KM, Hansen MT, Sonksen CP, Ludvigsen S, Raventos D, Buskov S, Christensen B, De Maria L, Taboureau O, Yaver D, Elvig-Jorgensen SG, Sorensen MV, Christensen BE, Kjaerulff S, Frimodt-Moller N, Lehrer RI, Zasloff M, Kristensen HH. Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. Nature. 2005 Oct 13;437(7061):975-80. PMID:16222292 doi:nature04051
  2. ↑ Xiang F, Xie Z, Feng J, Yang W, Cao Z, Li W, Chen Z, Wu Y. Plectasin, first animal toxin-like fungal defensin blocking potassium channels through recognizing channel pore region. Toxins (Basel). 2015 Jan 5;7(1):34-42. doi: 10.3390/toxins7010034. PMID:25568977 doi:http://dx.doi.org/10.3390/toxins7010034
  3. ↑ Mygind PH, Fischer RL, Schnorr KM, Hansen MT, Sonksen CP, Ludvigsen S, Raventos D, Buskov S, Christensen B, De Maria L, Taboureau O, Yaver D, Elvig-Jorgensen SG, Sorensen MV, Christensen BE, Kjaerulff S, Frimodt-Moller N, Lehrer RI, Zasloff M, Kristensen HH. Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. Nature. 2005 Oct 13;437(7061):975-80. PMID:16222292 doi:nature04051
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