| Literature DB >> 24564988 |
Takaaki Kinoshita1, Yosio Mori2, Kazumi Hirano1, Shinya Sugimoto3, Ken-ichi Okuda3, Shunsuke Matsumoto4, Takeshi Namiki5, Tatsuhiko Ebihara6, Masaaki Kawata6, Hidetoshi Nishiyama7, Mari Sato6, Mitsuo Suga7, Kenichi Higashiyama5, Kenji Sonomoto8, Yoshimitsu Mizunoe3, Shoko Nishihara1, Chikara Sato6.
Abstract
High-throughput immuno-electron microscopy is required to capture the protein-protein interactions realizing physiological functions. Atmospheric scanning electron microscopy (ASEM) allows in situ correlative light and electron microscopy of samples in liquid in an open atmospheric environment. Cells are cultured in a few milliliters of medium directly in the ASEM dish, which can be coated and transferred to an incubator as required. Here, cells were imaged by optical or fluorescence microscopy, and at high resolution by gold-labeled immuno-ASEM, sometimes with additional metal staining. Axonal partitioning of neurons was correlated with specific cytoskeletal structures, including microtubules, using primary-culture neurons from wild type Drosophila, and the involvement of ankyrin in the formation of the intra-axonal segmentation boundary was studied using neurons from an ankyrin-deficient mutant. Rubella virus replication producing anti-double-stranded RNA was captured at the host cell's plasma membrane. Fas receptosome formation was associated with clathrin internalization near the surface of primitive endoderm cells. Positively charged Nanogold clearly revealed the cell outlines of primitive endoderm cells, and the cell division of lactic acid bacteria. Based on these experiments, ASEM promises to allow the study of protein interactions in various complexes in a natural environment of aqueous liquid in the near future.Entities:
Mesh:
Year: 2014 PMID: 24564988 DOI: 10.1017/S1431927614000178
Source DB: PubMed Journal: Microsc Microanal ISSN: 1431-9276 Impact factor: 4.127