Чубик, Інна Ю.Чеботар, Сабіна ВіталіївнаChubyk, Inna Yu.Chebotar, Sabina V.2023-03-152023-03-152022Вісник Одеського національного університету = Odesa National University Heraldhttps://dspace.onu.edu.ua/handle/123456789/34644Проведено біоінформатичний аналіз нуклеотидних послідовностей «варіабельної області» генів адгезивного білка стопи мідій. Показано наявність в цій області мутацій, які дозволяють розрізняти між собою чотири види мідій: M. galloprovincialis, M. chilensis, M. edulis, M. trossulus. Використовуючи методи біоінформатики, проведено аналіз первинної та вторинної структури адгезивного білка мідії виду M. galloprovincialis, характерного для Чорноморського регіону, та побудовано модель тривимірної структури для зазначеного білка.Introduction. T oday, it is relevant to identify and study the genes of adhesive proteins that contribute to the adhesion of marine mussels under water and play an important role in the industry for the commercialization of waterproof adhesives. The purpose of our research is based on bioinformatic analysis, because modeling is currently one of the advanced methods. Aim. The purpose of this work was to compare the nucleotide sequences of representatives of the genus Mytilus, which are flanked by primers Me 15 / Me 16, designed for the non-repetitive region of the mussel adhesive protein gene, as well as bioinformatic analysis of the complete amino acid sequence of the foot adhesive protein Mefp‑1, coded by Fp1 gene by Fp1 gene, for M. galloprovincialis. Methods. Nucleotide sequences were analyzed using BLAST (NCBI [https://www. ncbi.nlm.nih.gov]) and aligned by MAFFT [Madeira et al., 2019] methods. The phylogenetic tree was built in the MEGA program [Kumar et al., 2018] using the UPGMA method [Sneath, Sokal, 1973]. The physicochemical parameters of the adhesive protein for the amino acid sequence of M. galloprovincialis were calculated using the ProtParam software tool (ExPASy [https://web.expasy.org/protparam/]). Models of the three-dimensional structure of the M. galloprovincialis adhesive protein were built on the I-TASSER online platform [Yang, Zhang, 2015; Zhang et al., 2018] and with application of the AlphaFold program [https://alphafold.ebi. ac.uk/entry/Q27409]. The main results. The analysis of the nucleotide sequences of six representatives of the genus Mytilus within the «variable region» flanked by primers Me 15 / Me 16 showed the presence of deletions and a number of SNPs. The constructed dendrogram reflected the phylogenetic relationships of mussel species in the genus Mytilus, when comparing the nucleotide sequences of the genes of the adhesive protein of the mussel foot. An analysis of the primary and secondary structure of the adhesive protein of the mussel species M. galloprovincialis characteristic of the Black Sea region was carried out, and model of the three-dimensional structure with correct global topology of the adhesive protein for the specified species was built. Conclusions. The detected mutations in the studied «variable region» of the nucleotide sequences of the adhesive protein genes allow the molecular marker Me 15–16 to distinguish between four types of mussels: M. galloprovincialis, M. chilensis, M. edulis, M. trossulus. The obtained distribution of representatives of the genus Mytilus by means of cluster analysis is consistent with the literature data on the territorial distribution of these species. The molecular weight was calculated and model of the foot adhesive protein of the mussel species M. galloprovincialis was constructed.ukMytilusген Fp1адгезивний білок мідіймолекулярний маркер Me 15–16біоінформатичний аналізgene Fp1adhesive protein of musselsmolecular marker Me 15–16bioinformatic analysisArticlehttps://doi.org/10.18524/2077–1746.2022.2(51).268553