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探索溶血素功能。

Towards Understanding the Function of Aegerolysins.

机构信息

Department of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, SI-1000 Ljubljana, Slovenia.

Department of Biology, Biotechnical Faculty, University of Ljubljana, SI-1000 Ljubljana, Slovenia.

出版信息

Toxins (Basel). 2022 Sep 11;14(9):629. doi: 10.3390/toxins14090629.

Abstract

Aegerolysins are remarkable proteins. They are distributed over the tree of life, being relatively widespread in bacteria and fungi, but also present in some insects, plants, protozoa, and viruses. Despite their abundance in cells of certain developmental stages and their presence in secretomes, only a few aegerolysins have been studied in detail. Their function, in particular, is intriguing. Here, we summarize previously published findings on the distribution, molecular interactions, and function of these versatile aegerolysins. They have very diverse protein sequences but a common fold. The machine learning approach of the AlphaFold2 algorithm, which incorporates physical and biological knowledge of protein structures and multisequence alignments, provides us new insights into the aegerolysins and their pore-forming partners, complemented by additional genomic support. We hypothesize that aegerolysins are involved in the mechanisms of competitive exclusion in the niche.

摘要

蜂毒素是一种显著的蛋白质。它们分布在生命之树上,在细菌和真菌中相对广泛存在,但也存在于一些昆虫、植物、原生动物和病毒中。尽管它们在某些发育阶段的细胞中大量存在,并且存在于分泌组中,但只有少数蜂毒素被详细研究过。它们的功能尤其令人好奇。在这里,我们总结了以前发表的关于这些多功能蜂毒素的分布、分子相互作用和功能的研究结果。它们的蛋白质序列非常多样化,但折叠方式相同。AlphaFold2 算法的机器学习方法,结合了蛋白质结构和多序列比对的物理和生物学知识,为我们提供了对蜂毒素及其孔形成伙伴的新见解,并辅以额外的基因组支持。我们假设蜂毒素参与了生态位竞争排斥的机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ab8/9505663/252c1cbd2fd4/toxins-14-00629-g001.jpg

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