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Antonets, K. S.

Publications and source records attributed to Antonets, K. S..

2 recordsLinked to original sources

Recombine and succeed: a story of Cry toxins to expand the host range

BackgroundCry toxins are the most widely used sources of bioinsecticides in agriculture; therefore, improving their functionality requires a deep understanding of natural evolution. It is thought that Cry toxins emerge via domain III swapping, yet the underlying mechanism remains unclear. ResultsWe detected 50 recombination events using a dataset of 368 clusters representing a known diversity of Cry toxins using a computational analysis. Not only do domain swaps engage all the domains, but they also occur continuously with approximately 70% of toxins participating in domain exchanges. Once they happen, hybrid toxins face purifying selection pressure reflecting the advantageous nature of receiving novel domains. When these domain exchanges occur, their host specificity changes dramatically. Strains housing these loci are enriched with cry genes and can kill a broader spectrum of hosts, thus implying that recombination allows them to occupy novel niches. The respective recombination-affected cry genes are flanked with insertions and harbor highly conservative blocks between the domains borders suggesting that the genomic context governs the intra-domain recombination. ConclusionsOur study expands the established views of the role of recombination in the emergence of Cry toxins. Here, we demonstrate that the domain exchanges shape both Cry sequences, the composition of toxins in bacterial strains, and the sets of hosts affected. The collected data allowed us to propose a mechanism for how these toxins originate. Overall, the results suggest that domain exchanges have a profound impact on Cry toxins being a major evolutionary driver.

bioinformatics↗

Accumulation of storage proteins in plant seeds is mediated by amyloid formation

Amyloids are protein aggregates with a highly ordered spatial structure giving them unique physicochemical properties. Different amyloids not only participate in the development of numerous incurable diseases but control vital functions in Archaea, Bacteria and Eukarya. Plants are a poorly studied systematic group in the field of amyloid biology. Amyloid properties have not yet been demonstrated for plant proteins under native conditions in vivo. Here we show that seeds of garden pea Pisum sativum L. contain amyloid-like aggregates of storage proteins, the most abundant one, 7S globulin Vicilin, forms bona fide amyloids in vivo and in vitro. The Vicilin amyloid accumulation increases during seed maturation and wanes at germination. Amyloids of Vicilin resist digestion by gastrointestinal enzymes, persist in canned peas and exhibit toxicity for yeast and mammalian cells. Our finding for the first time reveals involvement of amyloid formation in the accumulation of storage proteins in plant seeds.

biochemistry↗