Cargando…
Towards Understanding the Function of Aegerolysins
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, onl...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505663/ https://www.ncbi.nlm.nih.gov/pubmed/36136567 http://dx.doi.org/10.3390/toxins14090629 |
_version_ | 1784796529187356672 |
---|---|
author | Kraševec, Nada Skočaj, Matej |
author_facet | Kraševec, Nada Skočaj, Matej |
author_sort | Kraševec, Nada |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9505663 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-95056632022-09-24 Towards Understanding the Function of Aegerolysins Kraševec, Nada Skočaj, Matej Toxins (Basel) Review 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. MDPI 2022-09-11 /pmc/articles/PMC9505663/ /pubmed/36136567 http://dx.doi.org/10.3390/toxins14090629 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Kraševec, Nada Skočaj, Matej Towards Understanding the Function of Aegerolysins |
title | Towards Understanding the Function of Aegerolysins |
title_full | Towards Understanding the Function of Aegerolysins |
title_fullStr | Towards Understanding the Function of Aegerolysins |
title_full_unstemmed | Towards Understanding the Function of Aegerolysins |
title_short | Towards Understanding the Function of Aegerolysins |
title_sort | towards understanding the function of aegerolysins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505663/ https://www.ncbi.nlm.nih.gov/pubmed/36136567 http://dx.doi.org/10.3390/toxins14090629 |
work_keys_str_mv | AT krasevecnada towardsunderstandingthefunctionofaegerolysins AT skocajmatej towardsunderstandingthefunctionofaegerolysins |