AI Article Synopsis
- Secretory class V phospholipase A2 (PLA2-V) from chickens (ChPLA2-V) was expressed and characterized to understand its structure and function, revealing its crucial role in inflammation.
- The enzyme requires calcium for activity, performs best at pH 8.5 with phosphatidylcholine, and exhibits significant antibacterial and antifungal properties.
- Additionally, ChPLA2-V shows strong anticoagulant effects, making it a potential therapeutic agent for managing infections and blood coagulation issues.
Article Abstract
Secretory class V phospholipase A2 (PLA2-V) has been shown to be involved in inflammatory processes in cellular studies, but the biochemical and physical properties of this important enzyme have been unclear. As a first step towards understanding the structure, function and regulation of this PLA2, we report the expression and characterization of PLA2-V from chicken (ChPLA2-V). The ChPLA2-V cDNA was synthesized from chicken heart polyA mRNA by RT-PCR, and an expression construct containing the PLA2 was established. After expression in Pichia pastoris cells, the active enzyme was purified. The purified ChPLA2-V protein was biochemically and physiologically characterized. The recombinant ChPLA2-V has an absolute requirement for Ca for enzymatic activity. The optimum pH for this enzyme is pH 8.5 in Tris-HCl buffer with phosphatidylcholine as substrate. ChPLA2-V was found to display potent Gram-positive and Gram-negative bactericidal activity and antifungal activity in vitro. The purified enzyme ChPLA2-V with much stronger anticoagulant activity compared with the intestinal and pancreatic chicken PLA2-V was approximately 10 times more active. Chicken group V PLA2, like mammal one, may be considered as a future therapeutic agents against fungal and bacterial infections and as an anticoagulant agent.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.ijbiomac.2017.11.045 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Further Characterization of Lipase B from Ustilago maydis Expressed in Pichia pastoris: a Member of the Candida antarctica Lipase B-like Superfamily.
Appl Biochem Biotechnol
January 2025
Unidad de Biotecnología Industrial, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C, 45019, Zapopan, Jal, Mexico.
Lipases from the basidiomycete fungus Ustilago maydis are promising but underexplored biocatalysts due to their high homology with Candida antarctica lipases. This study provides a comprehensive characterization of a recombinant CALB-like lipase from U. maydis, expressed in Pichia pastoris (rUMLB), and compares its properties with those of the well-studied recombinant lipase B from C.
View Article and Find Full Text PDFDevelopment of a Recombinant Omicron BA.1 Subunit Vaccine Candidate in Pichia pastoris.
Microb Biotechnol
January 2025
Izmir Biomedicine and Genome Center, Izmir, Turkey.
Low-cost and safe vaccines are needed to fill the vaccine inequity gap for future pandemics. Pichia pastoris is an ideal expression system for recombinant protein production due to its cost-effective and easy-to-scale-up process. Here, we developed a next-generation SARS-CoV2 Omicron BA.
View Article and Find Full Text PDFStructural and Functional Glycosylation of the Abdala COVID-19 Vaccine.
Glycobiology
January 2025
Department of Biochemistry, Dorothy Crowfoot Hodgkin Building, University of Oxford, South Parks Road, OX1 3QU, United Kingdom.
Abdala is a COVID-19 vaccine produced in Pichia pastoris and is based on the receptor-binding domain (RBD) of the SARS-CoV-2 spike. Abdala is currently approved for use in multiple countries with clinical trials confirming its safety and efficacy in preventing severe illness and death. Although P.
View Article and Find Full Text PDFPromoted expression of a lipase for its application in EPA/DHA enrichment and mechanistic insights into its substrate specificity.
Int J Biol Macromol
January 2025
State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan 430062, PR China. Electronic address:
Expanding toolkits of EPA/DHA enrichment from natural sources is essential for better satisfying increasing demands for them. Lipase K80, from Proteus vulgaris K80, showed an application potential in EPA/DHA enrichment, whereas no desired heterologous expression in generally regarded as safe (GRAS) hosts restricted its relevant applications. In this study, expression of lipase K80 in a well-reputed GRAS host, Pichia pastoris, was achieved and further enhanced via combining disruption of its C-terminal KKL motif with co-expression of N-Acetyltransferase Mpr1, with a cumulative increment of nearly 200% in the secretion level and the volumetric activity.
View Article and Find Full Text PDFMicrobial Astaxanthin Synthesis by through Metabolic and Fermentation Engineering.
J Agric Food Chem
January 2025
State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211800, P.R. China.
Astaxanthin is a kind of carotenoid with a strong antioxidant ability, which has shown broad applications in the areas of healthcare, medicine, cosmetics, food additives, and aquaculture. With the increasing demand for natural products, the microbial production of astaxanthin has become a new hot spot. In this study, the astaxanthin synthesis pathway was first metabolically constructed in ()().
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!