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Journal of Virology, August 2008, p. 7346-7356, Vol. 82, No. 15
0022-538X/08/$08.00+0     doi:10.1128/JVI.00764-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Cryoelectron Microscopy Map of Atadenovirus Reveals Cross-Genus Structural Differences from Human Adenovirus{triangledown}

Radosav S. Pantelic,1 Linda J. Lockett,2 Rosalba Rothnagel,1 Ben Hankamer,1 and Gerald W. Both2*

Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia,1 CSIRO Molecular and Health Technologies, North Ryde, New South Wales 2113, Australia2

Received 8 April 2008/ Accepted 19 May 2008

A three-dimensional (3D) cryoelectron microscopy reconstruction of the prototype Atadenovirus (OAdV [an ovine adenovirus isolate]) showing information at a 10.6-Å resolution (0.5 Fourier shell correlation) was derived by single-particle analysis. This is the first 3D structure solved for any adenovirus that is not a Mastadenovirus, allowing cross-genus comparisons between structures and the assignment of genus-specific capsid proteins. Viable OAdV mutants that lacked the genus-specific LH3 and p32k proteins in purified virions were also generated. Negatively stained 3D reconstructions of these mutants were used to identify the location of protein LH3 and infer that of p32k within the capsid. The key finding was that LH3 is a critical protein that holds the outer capsid of the virus together. In its absence, the outer viral capsid is unstable. LH3 is located in the same position among the hexon subunits as its protein IX equivalent from mastadenoviruses but sits on top of the hexon trimers, forming prominent "knobs" on the virion surface that visually distinguish OAdV from other known AdVs. Electron density was also assigned to hexon and penton subunits and to proteins IIIa and VIII. There was good correspondence between OAdV density and human AdV hexon structures, which also validated the significant differences that were observed between the penton base protein structures.

* Corresponding author. Mailing address: CSIRO Molecular and Health Technologies, North Ryde, NSW 2113, Australia. Phone: 61 2 94905169. Fax: 61 2 98785121. E-mail: gerry.both{at}biotechequitypartners.com.au

{triangledown} Published ahead of print on 28 May 2008.

Journal of Virology, August 2008, p. 7346-7356, Vol. 82, No. 15
0022-538X/08/$08.00+0     doi:10.1128/JVI.00764-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Russell, W. C. (2009). Adenoviruses: update on structure and function. J. Gen. Virol. 90: 1-20 [Abstract] [Full Text]  


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