candida candida neoformans atcc 14116  (ATCC)

Journal: Frontiers in Pharmacology

Article Title: Phytochemical profiling, antimicrobial, antibiofilm, and molecular docking of Farsetia aegyptia and Zilla spinosa from Saudi Arabia

doi: 10.3389/fphar.2025.1723207

Figure Lengend Snippet: Anti-biofilm activity of F. aegyptia chloroformic sample (Fa CH), Z. spinosa chloroformic sample (Zs CH), F. aegyptia ethanolic sample (Fa ET), Z. spinosa ethanolic sample (Zs ET), F. aegyptia water sample (Fa W), and Z. spinosa water sample (Zs W) against (d) Candida albicans ATCC 90028, (e) Candida Krusei ATCC 6258, and (f) Candida neoformans ATCC 14116. The letters (a–p) on the bars present important differences (p < 0.05).

Article Snippet: Importantly, in the current study, all Gram-positive bacterial strains used, including S. aureus ATCC 25923, L. monocytogenes ATCC 19115, and E. faecalis ATCC 29212; Gram-negative bacterial strains comprising E. coli ATCC 35218, Salmonella Typhimurium ATCC 1408, and P. aeruginosa ATCC 27853, and strains of Candida : Candida neoformans ATCC 14116, Candida albicans ATCC 90028, and Candida krusei ATCC 6258, were considered biofilm producers according to the microtiter method results.

Techniques: Activity Assay

Journal: Frontiers in Pharmacology

Article Title: Phytochemical profiling, antimicrobial, antibiofilm, and molecular docking of Farsetia aegyptia and Zilla spinosa from Saudi Arabia

doi: 10.3389/fphar.2025.1723207

Figure Lengend Snippet: Anti-biofilm activity of F. aegyptia chloroformic sample (Fa CH), Z. spinosa chloroformic sample (Zs CH), F. aegyptia ethanolic sample (Fa ET), Z. spinosa ethanolic sample (Zs ET), F. aegyptia water sample (Fa W), and Z. spinosa water sample (Zs W) against (d) Candida albicans ATCC 90028, (e) Candida Krusei ATCC 6258, and (f) Candida neoformans ATCC 14116. The letters (a–p) on the bars present important differences (p < 0.05).

Article Snippet: The F. aegyptia and Z. spinosa chlorophormic, ethanolic, and water extracts were evaluated against three strains of Candida : Candida albicans ATCC 90028, Candida krusei ATCC 6258, and Candida neoformans ATCC 14116. presents the results of the disk diffusion method.

Techniques: Activity Assay

Journal: Nature Communications

Article Title: Coniontins, lipopetaibiotics active against Candida auris identified from a microbial natural product fractionation library

doi: 10.1038/s41467-025-62630-z

Figure Lengend Snippet: a Intracellular accumulation of coniotin A (CNA), caspofungin (CAP), and iturin A (ITA) in C. auris CBS10913 ( Cau ) and C. albicans ATCC90028 ( Cal ) after 10 min treatment. Data represent mean ± SD from four biological replicates. b Chitin levels in fungal cells after 4 h treatment with ½ MIC of CNA, CAP, or vehicle control (DMSO). Calcofluor white (CFW)-stained cells were analyzed by epifluorescence microscopy; bars represent the mean, with individual cell values (from three independent biological replicates) overlaid as dots. Statistical significance was determined using unpaired two-tailed t -tests with Welch’s correction; all comparisons between CNA and DMSO yielded P < 0.000001. c Representative CFW-stained images corresponding to ( b ). Scale bars, 10 µm. d Schematic of the Candida cell wall. Glycosylphosphatidylinositol-anchored mannoproteins form the outer layer linked to a β-glucan–chitin core. Echinocandins target the glucan synthase Fks1, compromising wall integrity. Created with BioRender.com. e Mannoprotein staining in C. albicans (ConA–Alexa Fluor 647) after treatment. Confocal 3D projections showing cell wall disruption (blue arrows). Scale bars, 5 µm. f Quantification of cell perimeter from treatments as in ( e ), based on ~150 cells (ImageJ). Significance was determined by a two-tailed unpaired Student’s t -test: exact P values are shown in the figure. g CNA binding to β−1,3-glucan and chitin assessed by mass spectrometry after pull-down assay. Relative abundance shown for bound (Glu-B, Chi-B) and unbound (Glu-S, Chi-S) fractions. Data represent mean ± SD of three biological replicates; each dot corresponds to one replicate. h CNA inhibits β−1,3-glucanase (GCase) digestion. Hexa-glucose oligosaccharides released from laminarin (a β−1,3-glucan) after 0.5 h hydrolysis with or without CNA (64, 128, or 256 µg/mL) were quantified by mass spectrometry. Data from three independent replicates are shown as dots; values are mean ± SD. Significance was determined using two-tailed unpaired t -tests with Welch’s correction. Exact P values are shown in the figure. i CNA inhibits β−1,3-glucan activation of Limulus factor G in a dose-dependent manner. β−1, 3-glucan (Glu) was incubated without/with CNA (0.625, 5, or 40 µg/mL; 1×, 8×, and 64×) and assayed using Glucatell®. Reactions were monitored at 405 nm for 1 h. Data represent mean ± SD from n = 3 independent biological replicates. j TEM of C. auris and C. neoformans ± CNA (½ MIC). CNA induces membrane detachment (blue arrowheads), loss of integrity (orange), and cell wall thickening. G + C β-glucan/chitin, M mannoprotein, N nucleus, m mitochondria. Scale bars, nm. Figures 5b, f–i, Source data and full statistical results are provided as a Source Data file.

Article Snippet: WAC11161 (this study), C. neoformans strain H99 (ATCC MYA-4901), C. auris (CBS10913, CBS12766, CBS12775, CBS12776; obtained from CBS-KNAW Fungal Biodiversity Centre), C. albicans (ATCC 90028, ATCC 200955), C. parapsilosis ATCC22019, C. tropicalis ATCC200956, C. glabrata CBS138 (formerly N. glabratus ; CBS-KNAW), S. cerevisiae BY4741 (ATCC 201388), and A. fumigatus (Af293, 1478) were cultured under standard eukaryotic conditions.

Techniques: Control, Staining, Epifluorescence Microscopy, Two Tailed Test, Disruption, Binding Assay, Mass Spectrometry, Pull Down Assay, Activation Assay, Incubation, Membrane