In this special issue.

Abstract

dynamics in Drosophila embryos, the tracking of cells and of cell division during the embryogenesis of zebrafish, in mice embryos, or brain as well as in plant tissues but also two-color pulse-chase-type imaging of molecules and mapping of proteins with photoacoustic and photothermal effects. With certain inherent limitations, the use of phototransformable fluorescent proteins for optical data storage has been shown to be feasible, and more realistic applications include ion, temperature, viscosity, and pH sensing. Christoph Cremer and colleagues (Cremer et al. 2014) report original work performed with a special localization microscopy method and spectral precision distance/position determination microscopy (SPDM) and demonstrate its great advantages for the analysis of both viral pathogens as well as virus-derived nanotools. SPDM with the use of standard fluorescent dyes in the visible spectrum and standard microscopic preparation techniques permitted the analysis of the aggregation state of modified tobacco mosaic virus particles with an accuracy of better than 8 nm. Dynamic parameters of virus–cell attachment and infection by influenza a virus as well as of various infection-related membrane proteins were analyzed with high precision by SPDM nanoimaging. Four perspectives for nanoimaging by SPDM are enumerated: virus–cell membrane interaction; expression of viral genes; optimization of (plant-) virus-based nanotools and biodetection devices; and identification of viruses by oligonucleotide labeling. related to this work are the studies by Patrick Muller and colleagues (Muller et al. 2014) on the spatial distribution and structural arrangement of a murine cytomegalovirus glycoprotein, gp36.5/ m164, as detected by SPDM localization microscopy. they show that by next neighbor distance analyses, appropriate characterization parameters for cellular structures and structural arrangements of cellular molecules can also be obtained from pure pointillist localization microscopy the second special issue of Histochem Cell Biol on single-molecule super-resolution microscopy covers various aspects of the application of this technique that have revolutionized the study of biological processes and structures at the nanoscale as pointed out in the Foreword by Jennifer lipincott-Schwartz. the topic is surveyed in two “review articles” and in seven “Original articles.” Hendrik Deschout, aleksandra radenovic, and their colleagues (Deschout et al. 2014) review recent progress in single-molecule resolution microscopy with emphasis on quantitative measurements such as counting of single molecules (i.e., NMDa receptors, glycine-gated channels, and asialo-glycoprotein receptor) with PalM, analysis of heterogeneity in the spatial organization of general membrane proteins or networks of signaling receptors and nuclear pore complexes, and single-molecule colocalization involving dual-color super-resolution microscopy to analyze, for example, protein–protein interactions. Both the potential of the technique and currently existing problems (i.e., limited detection efficiency, overcounting due to photoblinking, sample drift, localization uncertainty, and photoconversion efficiency of fluorescent proteins) using these tools are evaluated. Virgile adam (2014) focuses on the different classes of phototransformable fluorescent proteins and the variable applications for which they are useful. these applications include not only the monitoring of cellular