scholarly journals Microencapsulation of inorganic nanocrystals into PLGA microsphere vaccines enables their intracellular localization in dendritic cells by electron and fluorescence microscopy

2011 ◽  
Vol 151 (3) ◽  
pp. 278-285 ◽  
Author(s):  
Christopher Schliehe ◽  
Constanze Schliehe ◽  
Marc Thiry ◽  
Ulrich I. Tromsdorf ◽  
Joachim Hentschel ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Fluorescence Microscopy ◽  
Intracellular Localization ◽  
Plga Microsphere ◽  
Electron And Fluorescence Microscopy ◽  
Inorganic Nanocrystals

scholarly journals Intracellular localization of the mycobacterial stressosome complex

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Malavika Ramesh ◽  
Ram Gopal Nitharwal ◽  
Phani Rama Krishna Behra ◽  
B. M. Fredrik Pettersson ◽  
Santanu Dasgupta ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Fluorescence Microscopy ◽  
Bacillus Cereus ◽  
Intracellular Localization ◽  
Sigma Factors ◽  
Alternative Sigma Factors ◽  
Expression Of Genes ◽  
Molecular Machinery ◽  
Stress Signals ◽  
Activation Pathways

AbstractMicroorganisms survive stresses by alternating the expression of genes suitable for surviving the immediate and present danger and eventually adapt to new conditions. Many bacteria have evolved a multiprotein "molecular machinery" designated the "Stressosome" that integrates different stress signals and activates alternative sigma factors for appropriate downstream responses. We and others have identified orthologs of some of the Bacillus subtilis stressosome components, RsbR, RsbS, RsbT and RsbUVW in several mycobacteria and we have previously reported mutual interactions among the stressosome components RsbR, RsbS, RsbT and RsbUVW from Mycobacterium marinum. Here we provide evidence that "STAS" domains of both RsbR and RsbS are important for establishing the interaction and thus critical for stressosome assembly. Fluorescence microscopy further suggested co-localization of RsbR and RsbS in multiprotein complexes visible as co-localized fluorescent foci distributed at scattered locations in the M. marinum cytoplasm; the number, intensity and distribution of such foci changed in cells under stressed conditions. Finally, we provide bioinformatics data that 17 (of 244) mycobacteria, which lack the RsbRST genes, carry homologs of Bacillus cereus genes rsbK and rsbM indicating the existence of alternative σF activation pathways among mycobacteria.

scholarly journals MHC Class II levels and intracellular localization in human dendritic cells are regulated by calmodulin kinase II

2007 ◽  
Vol 82 (3) ◽  
pp. 686-699 ◽  
Author(s):  
Tara L. Herrmann ◽  
Reitu S. Agrawal ◽  
Sean F. Connolly ◽  
Ramona L. McCaffrey ◽  
Jamie Schlomann ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Mhc Class Ii ◽  
Intracellular Localization ◽  
Class Ii ◽  
Calmodulin Kinase ◽  
Human Dendritic Cells

Fluorescence Dynamics of Semiconductor Nanorod Clusters Studied by Correlated Atomic Force, Transmission Electron, and Fluorescence Microscopy

2008 ◽  
Vol 112 (50) ◽  
pp. 19945-19956 ◽  
Author(s):  
Claudia Querner ◽  
Siying Wang ◽  
Ken Healy ◽  
Jessamyn A. Fairfield ◽  
Michael D. Fischbein ◽  
...  
Keyword(s):  
Fluorescence Microscopy ◽  
Force Transmission ◽  
Atomic Force ◽  
Transmission Electron ◽  
Electron And Fluorescence Microscopy

Intracellular Localization of Two Betaine Lipids by Cell Fractionation and Immunomicroscopy

1997 ◽  
Vol 52 (7-8) ◽  
pp. 487-495 ◽  
Author(s):  
K. Department of Chemistry and Biochem ◽  
W. Department of Chemistry and Biochem ◽  
A. Faculty of Biology, University of B
Keyword(s):  
Fluorescence Microscopy ◽  
Cellular Localization ◽  
Gradient Centrifugation ◽  
Intracellular Localization ◽  
Rabbit Serum ◽  
Cell Fractionation ◽  
Thin Sections ◽  
Ochromonas Danica ◽  
Betaine Lipids ◽  
Cyt C

Abstract The cellular localization of the betaine lipids diacylglyceryl-N,N,N-trimethylhomoserine (DGTS) and diacylglycerylhydroxymethyl-N,N,N-trimethyl-β-alanine (DGTA) was investi­ gated by a) chemical analysis of subcellular fractions and b) immunochemical methods using specific antisera and either fluorescence microscopy or electron microscopy for detection of the label. A homogenate of Lycopodium annotinum (Pteridophyta) was fractionated by differential and density gradient centrifugation. The particulate fractions obtained were analyzed for chlorophyll, cyt c oxidase, NADH-cyt c reductase and DGTS. Non-plastidial fractions were enriched in DGTS and only minor amounts of this lipid could be attributed to chloroplasts. Anti-DGTS and anti-DGTA sera were produced by immunization of rabbits. The monospecificity of the antisera was examined with cells of Chlamydomonas reinhardtii (Chlorophyceae) containing DGTS, Pavlova lutheri (Haptophyceae) containing DGTA and Ochromonas danica (Chrysophyceae) containing both DGTS and DGTA. Euglena gracilis which is free of betaine lipids, was used as a control. For the test, a FITC-coupled goat anti-rabbit antibody was used and detected by fluorescence microscopy. Thin sections of Ochromonas and Pavlova were incubated first with the anti-lipid sera and subsequently with a gold-coupled anti-rabbit serum and then examined in the electron microscope. With O chro­ monas, anti-DGTS as well as anti-DGTA sera gave an accumulation of gold label in the cytoplasmic space but not in the chloroplasts. Similar results were obtained with Pavlova using anti-DGTA serum. These results describe for the first time the cytochemical localiza­ tion of DGTS and DGTA strongly suggesting both these lipids to be associated mainly with non-plastidial structures.

Study of ectoparasitism of ultramicrobacteria of the genus Kaistia, strains NF1 and NF3 by electron and fluorescence microscopy

Microbiology ◽  
2008 ◽  
Vol 77 (1) ◽  
pp. 47-54 ◽  
Author(s):  
N. E. Suzina ◽  
T. Z. Esikova ◽  
V. N. Akimov ◽  
T. N. Abashina ◽  
V. V. Dmitriev ◽  
...  
Keyword(s):  
Fluorescence Microscopy ◽  
Electron And Fluorescence Microscopy

scholarly journals SARS-CoV-2 spike protein S1 induces fibrin(ogen) resistant to fibrinolysis: Implications for microclot formation in COVID-19

2021 ◽  
Author(s):  
Lize M Grobbelaar ◽  
Chantelle Venter ◽  
Mare Vlok ◽  
Malebogo Ngoepe ◽  
Gert J Laubscher ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Blood Flow ◽  
Severe Acute Respiratory Syndrome ◽  
Fluorescence Microscopy ◽  
Clinical Relevance ◽  
Structural Changes ◽  
Spike Protein ◽  
Plasma Samples ◽  
Electron And Fluorescence Microscopy ◽  
Scanning Electron

Severe acute respiratory syndrome coronavirus 2 (SARS-Cov-2) -induced infection, the cause of coronavirus disease 2019 (COVID-19), is characterized by unprecedented clinical pathologies. One of the most important pathologies, is hypercoagulation and microclots in the lungs of patients. Here we study the effect of isolated SARS-CoV-2 spike protein S1 subunit as potential inflammagen sui generis. Using scanning electron and fluorescence microscopy as well as mass spectrometry, we investigate the potential of this inflammagen to interact with platelets and fibrin(ogen) directly to cause blood hypercoagulation.  Using platelet poor plasma (PPP), we show that spike protein may interfere with blood flow.  Mass spectrometry also showed that when spike protein S1 is added to healthy PPP, it results in structural changes to β and γ fibrin(ogen), complement 3, and prothrombin. These proteins were substantially resistant to trypsinization, in the presence of spike protein S1. Here we suggest that, in part, the presence of spike protein in circulation may contribute to the hypercoagulation in COVID-19 positive patients and may cause substantial impairment of fibrinolysis. Such lytic impairment may result in the persistent large microclots we have noted here and previously in plasma samples of COVID-19 patients. This observation may have important clinical relevance in the treatment of hypercoagulability in COVID-19 patients.

scholarly journals Dyskinetoplasty in two species of trypanosomatids

1979 ◽  
Vol 35 (1) ◽  
pp. 185-202
Author(s):  
S.L. Hajduk
Keyword(s):  
Fluorescence Microscopy ◽  
Kinetoplast Dna ◽  
Feulgen Staining ◽  
Crithidia Fasciculata ◽  
Caesium Chloride ◽  
Electron And Fluorescence Microscopy ◽  
Staining Techniques ◽  
Trypanosoma Equiperdum ◽  
In Cells

Dyskinetoplastic cells from both Crithidia fasciculata and Trypanosoma equiperdum lack detectable kinetoplast DNA (kDNA) by conventional staining techniques. Two dyskinetoplastic strains of T. equiperdum, either acriflavine-induced or spontaneously occurring, show normal amounts of kDNA (p = 1.692 g/cm3) in analytical caesium chloride, ultracentrifugation. Electron and fluorescence microscopy of the dyskinetoplastic strains of T. equiperdum suggest that the kDNA network is fragmented and dispersed throughout the mitochondrion. The fragmentation and dispersion of the kDNA, rather than a reduction in the amount of kDNA, is the cause of the lack of kinetoplast staining in the dyskinetoplastic strains of T. equiperdum. Acriflavine-treated cultures of C. fasciculata show a decrease in the amount of kDNA (p = 1.703 g/cm3) corresponding to the percentage of dyskinetoplastic cells in the cultures. Electron and fluorescence microscopy of acriflavine-treated cultures of C. fasciculata show the loss of the kDNA network in cells which lack Giemsa and Feulgen staining, confirming the hypothesis that the kDNA is lost in dyskinetoplastic trypanosomatids from insects. Possible modes of acriflavine action are considered and a proposed mechanism for acriflavine action in trypanosomes from mammals is presented.

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