Safety and potential allergenicity assessment of modified bacterial CA protein for transfer to plant in order to enhancing carbon sequestration efficiency
- سال انتشار: 1402
- محل انتشار: بیست و چهارمین کنگره بین المللی میکروب شناسی ایران
- کد COI اختصاصی: MEDISM24_398
- زبان مقاله: انگلیسی
- تعداد مشاهده: 29
نویسندگان
Department of Microbiology, Faculty of Biology, North Tehran Branch, Islamic Azad University, Tehran, Iran
Department of Biology, Faculty of Biology, North Tehran Branch, Islamic Azad University, Tehran, Iran
چکیده
BACKGROUND AND OBJECTIVESThe enzyme Carbonic anhydrase (CA) captures carbon by converting CO۲ to bicarbonate, which can serve as a carbon source for bacteria and plants .Various structures of this enzyme are found in organisms with different stability and efficiency. Transferring the optimized sequence of CA to bacteria and plants can improve carbon sequestration efficiency and enhance growth and metabolism .The purpose of this study is to evaluate the safety and potential allergenic effects of bacterial CA protein after codon optimization and its sequence modification in order to transfer to bacteria and plants to increase growth and metabolism efficiency.MATERIALS AND METHODSIn this study, the CA gene sequence of Caminibacter mediatlanticus bacterium was used. The codon-optimized and modified nucleotide sequence of CA, in FASTA format, was investigated in allergen databases including "AllERGEN ONLINE" and "ALLERMATCH". In this way, the complete sequence, ۸۰-amino acid sequences, and ۶-۸ amino acid sequences were compared with allergen sequences in the allergen database. Furthermore, the protein sequence was subjected to in silico enzyme digestion using pepsin, trypsin, and chymotrypsin in the "PEPTIDE CUTTER" database, and peptide fragments longer than eight amino acids were also examined in the allergy database .RESULTS AND DISCUSSIONThe homology analysis of the CA protein with various allergy databases showed no allergenicity. Furthermore, in silico enzyme digestion of this protein using pepsin, trypsin, and chymotrypsin generated ۳۹, ۳۲, and ۲۵ peptide fragments, respectively, with ۱۱, ۸, and ۱۰ fragments longer than ۸ amino acids. The examination of short peptide fragments was performed to investigate the possibility that peptide fragments larger than eight amino acids may act as epitope antigens. None of the resulting peptide fragments from the enzymatic digestion of the CA protein matched with the allergen peptides in the database.CONCLUSIONAccording to the WHO and FAO regulations, similarity of more than ۵۵% and ۹۵% for the full-length and ۸۰-amino acid sequences, respectively, with allergen sequences can be considered significant. Our results demonstrated the non-allergenic nature of this protein. Therefore, this study can address concerns related to the use of the modified sequence of this protein for transfer to different plant species .کلیدواژه ها
Allergenicity, Carbonic anhydrase, Modified protein, Safetyاطلاعات بیشتر در مورد COI
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