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ProteinQ1617783· pop 5· linked from 4 articles

Plectasin is an antibiotic protein from the mushroom Pseudoplectania nigrella. It was initially discovered in 2005 and commercialised by Novozymes. Plectasin belongs to the antimicrobial peptide class called fungal defensins, which is also present in invertebrates such as flies and mussels.

In the Vinony graph

Within Vinony's link graph, Plectasin is referenced by 4 other articles, and connects out to bacteria, antibiotic and invertebrate.

It is catalogued under topics including Antibiotics, Defensins and Peptides.

Its subject is documented across 4 Wikipedia language editions.

Protein · UniProt

Fungal defensin plectasin

Gene
DEF
Organism
Pseudoplectania nigrella (Ebony cup)
Length
95 aa
Molecular mass
10,254 Da
Evidence
1: Evidence at protein level

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 …

3D-structureAntibioticAntimicrobialCleavage on pair of basic residuesDefensinDirect protein sequencingDisulfide bondHost cell membrane
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Swiss-Prot (reviewed) · via UniProt

Wikidata facts

Instance of
protein
Image
Plectasin 3E7R.png
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Encyclopedic overview

2 sections
Contents
  • Clinical trials
  • References

Plectasin is an antibiotic protein from the mushroom Pseudoplectania nigrella. It was initially discovered in 2005 and commercialised by Novozymes. Plectasin belongs to the antimicrobial peptide class called fungal defensins, which is also present in invertebrates such as flies and mussels.

== Clinical trials == Pre-clinical tests in mice have shown promising results in that multiresistant bacteria have problems mutating resistance against plectasin, which acts by directly binding the bacterial cell-wall precursor Lipid II in a supramolecular complex.

Excerpted from Wikipedia’s “Plectasin” article, available under the CC BY-SA 4.0 licence.

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