October issue of Nature Biotechnology published an article about the latest trend in studying the high-throughput protein colocalization studies: multidimensional microscopic robot technology. The technology consists of cycles of fluorescence tagging, imaging and bleaching in situ. It is said that the technology combines three advances: a) a fluorescence technique capable of mapping hundreads of different proteins in one tissue section or sample, b) a method selecting the most prominent combinatorial molecular patterns by representing the data as binary vectors, c) and a system for imaging the distribution of these protein clusters in a so called toponome map. It is claimed that this approach is able to reveal rules of hierarchical protein network organization, in which state-specific lead proteins control protein network topology and function.
The method is relied on a so called multi-epitope-ligand cartography (MELC), that can map the location of several proteins in the one samlel of cells or tissue using sequential rounds of fluorescent detection in situ. Importantly, it appears that MELC can be used to show when and where proteins colocalize in cellular or tissue compartments, which proteins are excluded, how these associations are altered by pathology and how proteins are functionally interrelated.
MELC appears to be a significant step forward in colocalization analysis, because it enables obtaining considerably more reliable images for latter use with colocalization analysis software. It would be interesting to see whether these images will still require background correction, a critical step performed by the current software.
