The thionin family of antimicrobial peptides

Autor: Holger Bohlmann, Tina Austerlitz, Timo Bohlmann, Katharina Höng
Rok vydání: 2021
Předmět:
Leaves
Plant Science
Biochemistry
chemistry.chemical_compound
Amino Acids
Flowering Plants
Genetics
0303 health sciences
Multidisciplinary
biology
Organic Compounds
Plant Anatomy
030302 biochemistry & molecular biology
Eukaryota
Genomics
Plants
Chemistry
Papaver
Physical Sciences
Medicine
Transcriptome Analysis
Research Article
Pore Forming Cytotoxic Proteins
Science
Antimicrobial peptides
Research and Analysis Methods
Genome Complexity
03 medical and health sciences
Selaginella
Barley
Gene family
Sulfur Containing Amino Acids
Amino Acid Sequence
Cysteine
Grasses
Thionins
Molecular Biology Techniques
Molecular Biology
030304 developmental biology
Cloning
fungi
Organic Chemistry
Intron
Chemical Compounds
Organisms
Biology and Life Sciences
Proteins
Computational Biology
biology.organism_classification
Genome Analysis
Introns
Thionin
chemistry
Zdroj: PLoS ONE
PLoS ONE, Vol 16, Iss 7, p e0254549 (2021)
ISSN: 1932-6203
Popis: 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.
Databáze: OpenAIRE