Chemical Composition and in Vitro Antioxidant,Anti-Alzheimer,Anti-Diabetic,Anti-Tyrosinase,and Antimicrobial Properties of Essential Oils and Extracts Derived from Various Parts of the Algerian Calendula Suffruticosa Vahlsubsp. boissieri Lanza

Calendula suffruticosa Vahl subsp. boissieri Lanza is well-known for its medicinal properties in northeastern Algeria. As far as literature has been able to prove, no study has attempted to make a phytochemical or biological activity evaluation (antioxidants, enzyme inhibitors and antimicrobial potential). This work intends to evaluate, for the first time, the chemical constituents and study the previously mentioned biological activities of C. suffruticosa boissieri essential oil and different sections (flowers, leaves, roots) as well as the effect of changing the solvent (ethanol 70 %) and (methanol 70 %) on these activities. The essential oil of aerial parts of this plant was investigated using GC/MS, and 45 compounds were discovered, accounting for 98.01 % of the essential oil, including 23 monoterpenes, 6 sesquiterpenes, 12 diterpenes, 1 coumarin, 3 alkanes, methyl-cyclohexane (23.73 %), limonene (25.02 %), and o-cymene (13.20 %). Five methods were used to study the antioxidant activity (ABTS, DPPH, CUPRAC, reducing power, and β-carotene bleaching assay), where the results were impressive, especially for the essential oil. In addition, the hydroethanolic solvent (70 %) was found to be the most effective solvent for extraction in general compared to the hydromethanolic solvent (70 %). The extracts and essential oils of C. suffruticosa boissieri also showed a strong inhibiting ability against cholinesterase, tyrosinase, anti-α-amylase, α-glucosidase, and antimicrobials, a very valuable antioxidant, which is a real discovery. Based on these results, it can be said that this plant has important biological activities, so it can be used in the phytotherapy, food, or pharmaceutical sectors.     

Internalin must be on the bacterial surface to mediate entry of Listeria monocytogenes into epithelial cells

Entry of Listeria monocytogenes into cultured epithelial cells requires production of internalin, a protein with features characteristic of some Gram-positive bacterial surface proteins, in particular an LPXTG motif preceding a hydrophobic sequence and a few basic residues at its C-terminal end. By immunofluorescence and immunogold labelling, we show that in wild-type L. monocytogenes, internalin is present on the cell surface and has a polarized distribution similar to that of ActA, another surface protein of L. monocytogenes involved in actin assembly. Through a genetic analysis, we establish that the C-terminal region of internalin is necessary for cell-surface association, and that although internalin is partially released in the culture medium, its location on the bacterial surface is required to promote entry. Finally, using a‘domain-swapping’strategy - replacement of the cell wall anchor of InIA by the membrane anchor of ActA - we show that the reduced ability to adhere and enter cells of strains expressing InIA-ActA correlates with a lower amount of surface-exposed internalin. Taken together, these results suggest that internalin exposed on the bacterial surface mediates direct contact between the bacterium and the host cell.