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Spices as Eco-friendly Microbicides: From Kitchen to Clinic
Published in Mahendra Rai, Chistiane M. Feitosa, Eco-Friendly Biobased Products Used in Microbial Diseases, 2022
Allicin is a chemically oxygenated sulfur amino acid that occurs as a major component of garlic extract and has potent in vitro antimicrobial activity. Bacterial species like methicillin-resistant Staphylococcus aureus, Escherichia coli, Enterococcus, Shigella dysenteriae, S. flexneri, and S. sonnei are sensitive while Pseudomonas aeruginosa, Streptococcus β hemolyticus and Enterococcus faecium, are resistant to allicin (Ankri and Mirelman 1999). According to Yamada and Azuma (1977) pure allicin possess fungistatic and fungicidal activity against Candida, Cryptococcus, Trichophyton, Epidermophyton, and Microsporum at low concentration with MIC between 1.57 and 6.25 µg/mL. Allicin reacts with thiol compound (L-cysteine) to form the S-thiolation product, S-allylmercaptocysteine. However the main antimicrobial effect of allicin is due to its interaction with important thiol-containing enzymes. Allicin also specifically inhibits other bacterial enzymes such as the acetyl-CoA-forming system, consisting of acetate kinase and phosphotransacetyl-CoA synthetase. The wide spectrum antimicrobial effects of allicin are due to the multiple inhibitory effects they may have on various thiol-dependent enzymatic systems.
Cell division cycle protein 42 regulates the inflammatory response in mice bearing inflammatory bowel disease
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2019
Le-Mei Dong, Xiao-Wei Chen, Xi-Xi He, Xue-Pei Jiang, Fang Wu
Cell division cycle protein 42 (CDC42) is a small-molecule switch protein, whose main function is to affect cell migration and polarity by regulating actin rearrangement [4]. CDC42 can regulate the differentiation of immune cells [5]. Moreover, CDC42 has great influence on macrophages. It participates in the regulation of the phagocytosis and migration of macrophage [5,6]. It binds to target proteins: (i) such as nonkinases-Wiskott-Aldrich syndrome proteins (WASPs), partitioning-defective protein 6 (PAR6), and IQ-motif-containing GTPase-activating proteins (IQGAPs) to regulate vesicle trafficking, cytoskeletal reorganization, and cell polarization; (ii) such as lipid kinase-phosphatidylinositol 3-kinase (PI3K) to regulate cell mitosis; (iii) such as serine/threonine kinases-p21-activated kinase (PAK), S6 kinase (S6K), mixed lineage kinase 3 (MLK3) to regulate transcriptional activity, cell cycle, and cytoskeletal reorganization; (iv) such as tyrosine kinase-acetate kinase (ACK) to regulate receptor-mediated endocytosis [7–9].
Opportunistic bacteria confer the ability to ferment prebiotic starch in the adult cystic fibrosis gut
Published in Gut Microbes, 2019
Yanan Wang, Lex E.X. Leong, Rebecca L. Keating, Tokuwa Kanno, Guy C.J. Abell, Fredrick M. Mobegi, Jocelyn M. Choo, Steve L. Wesselingh, A. James Mason, Lucy D. Burr, Geraint B. Rogers
In contrast to butyrate and propionate, post-fermentation levels of acetate were significantly reduced in CF reactions compared with healthy controls. Acetate can be synthesised by a number of enteric bacteria52 mainly via the CoA-transferase pathway, involving the combined activities of phosphotransacetylase (PTA) and acetate kinase (AckA).53 Acetate production in healthy controls was positively correlated with the relative abundance of Anaerostipes and Dorea genera; taxa that were substantially less prevalent in post-fermentation CF microbiota. The combination of reduced levels of genes encoding acetate biosynthesis, and a low prevalence of taxa that are able to metabolise acetate (e.g. Faecalibacterium, Roseburia and Coprococcus), suggests that acetate levels in CF reactions reflected reduced production, rather than increased bacterial utilisation.
Bile acid oxidation by Eggerthella lenta strains C592 and DSM 2243T
Published in Gut Microbes, 2018
Spencer C. Harris, Saravanan Devendran, Celia Méndez- García, Sean M. Mythen, Chris L. Wright, Christopher J. Fields, Alvaro G. Hernandez, Isaac Cann, Phillip B. Hylemon, Jason M. Ridlon
Genes encoding enzymes in the methyl branch of the WLP were also identified in the genomes of E. lenta DSM 2243 and E. lenta sp. strain C592 including formate dehydrogenase (fdh) (Elen_3031; CAB18_RS01995), which flanks the ACS/CODH cluster, formyl-tetrahydrofolate synthase (fsh) (Elen_2864; CAB18_RS01970), methylene-tetrahydrofolate dehydrogenase/cyclohydrolase (folD) (Elen_2861; CAB18_RS01985), bifunctional homocysteine S-methyltransferase/5,10-methylene-tetrahydrofolate reductase (yitJ) (Elen_2573; CAB18_RS03325). These results provide a plausible explanation for why E. lenta oxidizes bile acids in a reducing environment: oxidation of bile acids provides reducing equivalents for the fixation of CO2 to acetate. Genes encoding enzymes involved in the energy conservation by substrate-level phosphorylation resulting in the conversion of acetyl-CoA to acetyl-PO4 (eutD) (Elen_1728, and acetate kinase (ackA) (Elen_1729; CAB18_RS07170) were also identified. We also located pyruvate:ferrodoxin oxidoreductase (PFOR) in both E. lenta DSM 2243 (Elen_2140) and several annotated genes for PFOR in E. lenta C592 (CAB18_RS00220; CAB18_RS05160; CAB18_RS07295; CAB18_RS07920; CAB18_RS13765). PFOR links the Wood-Ljungdahl pathway to the reductive tricarboxylic acid cycle, allowing autotrophic biosynthesis of complex macromolecules.44