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21. Characterization of Escherichia coli Strains for Novel Production of Plasmodium ovale Lactate Dehydrogenase.

Author

Choi, Jae-Won, Ha, Sang-Oh, Kim, Yeon-Jun, Shin, Jun-Seop, Choi, Min-Ji, Yu, Si-Eun, Han, Junghun, Park, Eun-Ji, Park, Kyoung Sik, and Kang, Jung Hoon

Subjects
LACTATE dehydrogenase, ESCHERICHIA coli, PLASMODIUM, MOLECULAR cloning, PLASMODIUM vivax, RECOMBINANT proteins
Abstract

Malaria is one of the most prevalent diseases worldwide with high incidence and mortality. Among the five species that can infect humans, Plasmodium ovale morphologically resembles Plasmodium vivax, resulting in misidentification and confusion in diagnosis, and is responsible for malarial disease relapse due to the formation of hypnozoites. P. ovale receives relatively less attention compared to other major parasites, such as P. falciparum and P. vivax, primarily due to its lower pathogenicity, mortality rates, and prevalence rates. To efficiently produce lactate dehydrogenase (LDH), a major target for diagnosing malaria, this study used three Escherichia coli strains, BL21(DE3), BL21(DE3)pLysS, and Rosetta(DE3), commonly used for recombinant protein production. These strains were characterized to select the optimal strain for P. ovale LDH (PoLDH) production. Gene cloning for recombinant PoLDH production and transformation of the three strains for protein expression were performed. The optimal PoLDH overexpression and washing buffer conditions in nickel-based affinity chromatography were established to ensure high-purity PoLDH. The yields of PoLDH expressed by the three strains were as follows: BL21(DE3), 7.6 mg/L; BL21(DE3)pLysS, 7.4 mg/L; and Rosetta(DE3), 9.5 mg/L. These findings are expected to be highly useful for PoLDH-specific diagnosis and development of antimalarial therapeutics. [ABSTRACT FROM AUTHOR]

Published
2024
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39. An effective datasets describing antimicrobial peptide produced from Pediococcus acidilactici - purification and mode of action determined by molecular docking

Author

Ramachandran Chelliah, Kandasamy Saravanakumar, Eric Banan-Mwine Daliri, Joong-Hark Kim, Jung-Kun Lee, Hyeon-yeong Jo, Inamul Hasan Madar, Se-Hun Kim, Sudha Rani Ramakrishnan, Momna Rubab, Kaliyan Barathikannan, Fred Kwame Ofosu, Hwang Subin, Park Eun-ji, Fazle Elahi, Myeong-Hyeon Wang, and Deog-Hwan Oh

Subjects
antimicrobial peptide, mode of action, structural characterization, gene expression, primers designed based on protein motif, identification of antimicrobial peptide or functional peptide, Computer applications to medicine. Medical informatics, R858-859.7, Science (General), Q1-390
Abstract

Most of the probiotics Bacterial cells, express native antibacterial genes, resulting in the production of, antimicrobial peptides, which have various applications in biotechnology and drug development. But the identification of antibacterial peptide, structural characterization of antimicrobial peptide and prediction on mode of action. Regardless of the significance of protein manufacturing, three individual factors are required for the production method: gene expression, stabilization and specific peptide purification. Our protocol describes a straightforward technique of detecting and characterizing particular extracellular peptides and enhancing the antimicrobial peptide expression we optimized using low molecular weight peptides. This protocol can be used to improve peptide detection and expression. The following are the benefits of this method, (DOI – https://doi.org/10.1016/j.ijbiomac.2019.10.196 [1]).The data briefly describe a simple method in detection identification, characterization of antimicrobial extracellular peptide, predicating the mode of action of peptide in targeting pathogens (In-silico method), brief method on profiling of antimicrobial peptide and its mode of action [1]. Further the protocol can be used to enhance the specific peptide expressions, detection of peptides. The advantages of this technique are presented below: • Characterization protocol of specific antimicrobial peptide • The folded antimicrobial peptide expression were less expressed or non-expressed peptides. • Besides being low cost, less time-consuming, easy to handle, universal and fast to execute, the suggested technique can be used for multiple proteins expressed in probiotics (Lactobacillus species) expression system.

Published
2020
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