Literature DB >> 9361260

IRIS explorer software for radial-depth cueing reovirus particles and other macromolecular structures determined by cryoelectron microscopy and image reconstruction.

S M Spencer1, J Y Sgro, K A Dryden, T S Baker, M L Nibert.   

Abstract

Structures of biological macromolecules determined by transmission cryoelectron microscopy (cryo-TEM) and three-dimensional image reconstruction are often displayed as surface-shaded representations with depth cueing along the viewed direction (Z cueing). Depth cueing to indicate distance from the center of virus particles (radial-depth cueing, or R cueing) has also been used. We have found that a style of R cueing in which color is applied in smooth or discontinuous gradients using the IRIS Explorer software is an informative technique for displaying the structures of virus particles solved by cryo-TEM and image reconstruction. To develop and test these methods, we used existing cryo-TEM reconstructions of mammalian reovirus particles. The newly applied visualization techniques allowed us to discern several new structural features, including sites in the inner capsid through which the viral mRNAs may be extruded after they are synthesized by the reovirus transcriptase complexes. To demonstrate the broad utility of the methods, we also applied them to cryo-TEM reconstructions of human rhinovirus, native and swollen forms of cowpea chlorotic mottle virus, truncated core of pyruvate dehydrogenase complex from Saccharomyces cerevisiae, and flagellar filament of Salmonella typhimurium. We conclude that R cueing with color gradients is a useful tool for displaying virus particles and other macromolecules analyzed by cryo-TEM and image reconstruction.

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Year:  1997        PMID: 9361260     DOI: 10.1006/jsbi.1997.3902

Source DB:  PubMed          Journal:  J Struct Biol        ISSN: 1047-8477            Impact factor:   2.867


  7 in total

Review 1.  Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs.

Authors:  T S Baker; N H Olson; S D Fuller
Journal:  Microbiol Mol Biol Rev       Date:  1999-12       Impact factor: 11.056

2.  Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A.

Authors:  Xing Zhang; Stephen B Walker; Paul R Chipman; Max L Nibert; Timothy S Baker
Journal:  Nat Struct Biol       Date:  2003-11-09

3.  Thermolabilizing pseudoreversions in reovirus outer-capsid protein micro 1 rescue the entry defect conferred by a thermostabilizing mutation.

Authors:  Melina A Agosto; Jason K Middleton; Elaine C Freimont; John Yin; Max L Nibert
Journal:  J Virol       Date:  2007-05-16       Impact factor: 5.103

4.  Effects of viscogens on RNA transcription inside reovirus particles.

Authors:  Aleksander A Demidenko; Jinkee Lee; Thomas R Powers; Max L Nibert
Journal:  J Biol Chem       Date:  2011-06-30       Impact factor: 5.157

5.  Disulfide bonding among micro 1 trimers in mammalian reovirus outer capsid: a late and reversible step in virion morphogenesis.

Authors:  Amy L Odegard; Kartik Chandran; Susanne Liemann; Stephen C Harrison; Max L Nibert
Journal:  J Virol       Date:  2003-05       Impact factor: 5.103

6.  Sequence Conservation, Radial Distance and Packing Density in Spherical Viral Capsids.

Authors:  Chih-Min Chang; Yu-Wen Huang; Chi-Wen Lee; Tsun-Tsao Huang; Chung-Shiuan Shih; Jenn-Kang Hwang
Journal:  PLoS One       Date:  2015-07-01       Impact factor: 3.240

7.  Reovirus directly engages integrin to recruit clathrin for entry into host cells.

Authors:  Melanie Koehler; Simon J L Petitjean; Jinsung Yang; Pavithra Aravamudhan; Xayathed Somoulay; Cristina Lo Giudice; Mégane A Poncin; Andra C Dumitru; Terence S Dermody; David Alsteens
Journal:  Nat Commun       Date:  2021-04-12       Impact factor: 14.919

  7 in total

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