Understanding Diversity, Evolution, and Structure of Small Heat Shock Proteins in Annelida Through in Silico Analyses
Basic science published in Front Physiol (2022)
Abstract
Small heat shock proteins (sHsps) are oligomeric stress proteins characterized by an α-crystallin domain (ACD). These proteins are localized in different subcellular compartments and play critical roles in the stress physiology of tissues, organs, and whole multicellular eukaryotes. They are ubiquitous proteins found in all living organisms, from bacteria to mammals, but they have never been studied in annelids. Here, a data set of 23 species spanning the annelid tree of life, including mostly transcriptomes but also two genomes, was interrogated and 228 novel putative sHsps were identified and manually curated. The analysis revealed very high protein diversity and showed that a significant number of sHsps have a particular dimeric architecture consisting of two tandemly repeated ACDs. The phylogenetic analysis distinguished three main clusters, two of them containing both monomeric sHsps, and ACDs located downstream in the dimeric sHsps, and the other one comprising the upstream ACDs from those dimeric forms. Our results support an evolutionary history of these proteins based on duplication events prior to the Spiralia split. Monomeric sHsps 76) were further divided into five subclusters. Physicochemical properties, subcellular location predictions, and sequence conservation analyses provided insights into the differentiating elements of these putative functional groups. Strikingly, three of those subclusters included sHsps with features typical of metazoans, while the other two presented characteristics resembling non-metazoan proteins. This study provides a solid background for further research on the diversity, evolution, and function in the family of the sHsps. The characterized annelid sHsps are disclosed as essential for improving our understanding of this important family of proteins and their pleotropic functions. The features and the great diversity of annelid sHsps position them as potential powerful molecular biomarkers of environmental stress for acting as prognostic tool in a diverse range of environments.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Резюме
228 small heat shock proteins identified across 23 annelid species including leeches reveal dimeric ACD architectures and three phylogenetic clusters supporting environmental stress biomarker potential.
Почему это важно для гирудотерапии
This in-silico study interrogated transcriptomes and genomes of 23 annelid species to identify and characterize 228 novel small heat shock proteins (sHsps), revealing high diversity, a distinctive tandemly duplicated α-crystallin domain architecture in many sequences, three main phylogenetic clusters, and physicochemical/subcellular features that may serve as environmental stress biomarkers. The work has only indirect relevance to ASH: it concerns annelid biology writ large and medicinal leeches (Hirudo) are not separately singled out, nor are secretome or hirudotherapy components examined. The honest caveat is that this is a computational/evolutionary study with no wet-lab, secretome, pharmacology, or clinical content, so its practical relevance to hirudotherapy is limited to foundational annelid biology.
Цитирование
Understanding Diversity, Evolution, and Structure of Small Heat Shock Proteins in Annelida Through in Silico Analyses.
de la Fuente M, Novo M · Frontiers in physiology, 2022
Связанный клинический контекст
Узнайте, как это исследование связано с клинической практикой
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