The thionin family of antimicrobial peptides.

Thionins are antimicrobial peptides found only in plants. They are first produced as preproproteins and then processed to yield the usually 5 kDa, basic thionin peptide with three or four disulfide bridges. So far, thionins had only been found in some plant families of angiosperms. The One Thousand...

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Autores principales: Katharina Höng, Tina Austerlitz, Timo Bohlmann, Holger Bohlmann
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Publicado: Public Library of Science (PLoS) 2021
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spelling oai:doaj.org-article:f336b6749b53466088cce35a752fb4182021-12-02T20:07:01ZThe thionin family of antimicrobial peptides.1932-620310.1371/journal.pone.0254549https://doaj.org/article/f336b6749b53466088cce35a752fb4182021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0254549https://doaj.org/toc/1932-6203Thionins are antimicrobial peptides found only in plants. They are first produced as preproproteins and then processed to yield the usually 5 kDa, basic thionin peptide with three or four disulfide bridges. So far, thionins had only been found in some plant families of angiosperms. The One Thousand Plant Transcriptomes Initiative (1KP project) has sequenced the transcriptomes of more than 1000 plant species. We have used these data to search for new thionin sequences which gave 225 hits. After removing doublets these resulted in 133 new thionins. No sequences were found in algae and mosses. The phylogenetically earliest hits were from Selaginella species and from conifers. Many hits were from angiosperm plant families which were previously not known to contain thionins. A large gene family for thionins was found in Papaver. We isolated a genomic clone from Papaver somniferum which confirmed the general genomic structure with two small introns within the acidic domain. We also expressed the thionin encoded by the genomic clone and found that it had antimicrobial activity in vitro, especially against fungi. Previously, we had grouped thionins into four classes. The new data reported here led us to revise this classification. We now recognize only class 1 thionins with eight cysteine residues and class 2 thionins with six cysteine residues. The different variants that we found (and also previously known variants) can all be traced back to one of these two classes. Some of the variants had an uneven number of cysteine residues and it is not clear at the moment what that means for their threedimensional structure.Katharina HöngTina AusterlitzTimo BohlmannHolger BohlmannPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 7, p e0254549 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Katharina Höng
Tina Austerlitz
Timo Bohlmann
Holger Bohlmann
The thionin family of antimicrobial peptides.
description Thionins are antimicrobial peptides found only in plants. They are first produced as preproproteins and then processed to yield the usually 5 kDa, basic thionin peptide with three or four disulfide bridges. So far, thionins had only been found in some plant families of angiosperms. The One Thousand Plant Transcriptomes Initiative (1KP project) has sequenced the transcriptomes of more than 1000 plant species. We have used these data to search for new thionin sequences which gave 225 hits. After removing doublets these resulted in 133 new thionins. No sequences were found in algae and mosses. The phylogenetically earliest hits were from Selaginella species and from conifers. Many hits were from angiosperm plant families which were previously not known to contain thionins. A large gene family for thionins was found in Papaver. We isolated a genomic clone from Papaver somniferum which confirmed the general genomic structure with two small introns within the acidic domain. We also expressed the thionin encoded by the genomic clone and found that it had antimicrobial activity in vitro, especially against fungi. Previously, we had grouped thionins into four classes. The new data reported here led us to revise this classification. We now recognize only class 1 thionins with eight cysteine residues and class 2 thionins with six cysteine residues. The different variants that we found (and also previously known variants) can all be traced back to one of these two classes. Some of the variants had an uneven number of cysteine residues and it is not clear at the moment what that means for their threedimensional structure.
format article
author Katharina Höng
Tina Austerlitz
Timo Bohlmann
Holger Bohlmann
author_facet Katharina Höng
Tina Austerlitz
Timo Bohlmann
Holger Bohlmann
author_sort Katharina Höng
title The thionin family of antimicrobial peptides.
title_short The thionin family of antimicrobial peptides.
title_full The thionin family of antimicrobial peptides.
title_fullStr The thionin family of antimicrobial peptides.
title_full_unstemmed The thionin family of antimicrobial peptides.
title_sort thionin family of antimicrobial peptides.
publisher Public Library of Science (PLoS)
publishDate 2021
url https://doaj.org/article/f336b6749b53466088cce35a752fb418
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