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Title

Hexavalent capsomers of herpes simplex virus type 2 : symmetry, shape, dimensions, and oligomeric status
Authors
Steven, Alasdair C.
Roberts, C. R.
Hay, J
Bisher, ME
Pun, Thierry
Trus, Benes L.
Published in Journal of Virology. 1986, vol. 57, no. 2, p. 578-584
Abstract The structures of the hexavalent capsomers of herpes simplex virus type 2 were analyzed by negative staining electron microscopy of capsomer patches derived from partially disrupted nucleocapsids. Optimally computer-averaged images were formed for each of the three classes of capsomer distinguished by their respective positions on the surface of the icosahedral capsid with a triangulation number of 16; in projection, each capsomer exhibited unequivocal sixfold symmetry. According to correspondence analysis of our set of capsomer images, no significant structural differences were detected among the three classes of capsomers, as visualized under these conditions. Taking into account information from images of freeze-dried, platinum-shadowed nucleocapsid fragments, it was established that each hexavalent capsomer is a hexamer of the 155-kilodalton major capsid protein. The capsomer has the form of a sixfold hollow cone approximately 12 nm in diameter and approximately 15 nm in depth, whose axial channel tapers in width from the outside towards the inner capsid surface.
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Other version: http://jvi.asm.org/content/57/2/578.full.pdf+html
Structures
Faculté des sciences / Département d'informatique
Centres et instituts / Centre universitaire d'informatique
Research groups Computer Vision and Multimedia Laboratory
Multimodal Interaction Group
Citation
(ISO format) 		STEVEN, Alasdair C. et al. Hexavalent capsomers of herpes simplex virus type 2 : symmetry, shape, dimensions, and oligomeric status. In: Journal of Virology, 1986, vol. 57, n° 2, p. 578-584. https://archive-ouverte.unige.ch/unige:47450

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Deposited on : 2015-03-03

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