This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Saban, S. D.
Right arrow Articles by Stewart, P. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Saban, S. D.
Right arrow Articles by Stewart, P. L.

 Previous Article  |  Next Article 

Journal of Virology, December 2006, p. 12049-12059, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.01652-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Visualization of {alpha}-Helices in a 6-Ångstrom Resolution Cryoelectron Microscopy Structure of Adenovirus Allows Refinement of Capsid Protein Assignments{triangledown} ,{dagger}

Susan D. Saban,1 Mariena Silvestry,1 Glen R. Nemerow,2 and Phoebe L. Stewart1*

Department of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, 2215 Garland Avenue, Nashville, Tennessee 37232,1 Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, IMM-19, La Jolla, California 920372

Received 1 August 2006/ Accepted 15 September 2006

The structure of adenovirus was determined to a resolution of 6 Å by cryoelectron microscopy (cryoEM) single-particle image reconstruction. Docking of the hexon and penton base crystal structures into the cryoEM density established that {alpha}-helices of 10 or more residues are resolved as rods. A difference map was calculated by subtracting a pseudoatomic capsid from the cryoEM reconstruction. The resulting density was analyzed in terms of observed {alpha}-helices and secondary structure predictions for the additional capsid proteins that currently lack atomic resolution structures (proteins IIIa, VI, VIII, and IX). Protein IIIa, which is predicted to be highly {alpha}-helical, is assigned to a cluster of helices observed below the penton base on the inner capsid surface. Protein VI is present in ~1.5 copies per hexon trimer and is predicted to have two long {alpha}-helices, one of which appears to lie inside the hexon cavity. Protein VIII is cleaved by the adenovirus protease into two fragments of 7.6 and 12.1 kDa, and the larger fragment is predicted to have one long {alpha}-helix, in agreement with the observed density for protein VIII on the inner capsid surface. Protein IX is predicted to have one long {alpha}-helix, which also has a strongly indicated propensity for coiled-coil formation. A region of density near the facet edge is now resolved as a four-helix bundle and is assigned to four copies of the C-terminal {alpha}-helix from protein IX.

* Corresponding author. Mailing address: Vanderbilt University Medical Center, Department of Molecular Physiology and Biophysics, 710 Light Hall, 2215 Garland Ave., Nashville, TN 37232. Phone: (615) 322-7908. Fax: (615) 322-7236. E-mail: phoebe.stewart{at}vanderbilt.edu.

{triangledown} Published ahead of print on 27 September 2006.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, December 2006, p. 12049-12059, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.01652-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lindert, S., Silvestry, M., Mullen, T.-M., Nemerow, G. R., Stewart, P. L. (2009). Cryo-Electron Microscopy Structure of an Adenovirus-Integrin Complex Indicates Conformational Changes in both Penton Base and Integrin. J. Virol. 83: 11491-11501 [Abstract] [Full Text]  
  • Silvestry, M., Lindert, S., Smith, J. G., Maier, O., Wiethoff, C. M., Nemerow, G. R., Stewart, P. L. (2009). Cryo-Electron Microscopy Structure of Adenovirus Type 2 Temperature-Sensitive Mutant 1 Reveals Insight into the Cell Entry Defect. J. Virol. 83: 7375-7383 [Abstract] [Full Text]  
  • Fabry, C. M. S., Rosa-Calatrava, M., Moriscot, C., Ruigrok, R. W. H., Boulanger, P., Schoehn, G. (2009). The C-Terminal Domains of Adenovirus Serotype 5 Protein IX Assemble into an Antiparallel Structure on the Facets of the Capsid. J. Virol. 83: 1135-1139 [Abstract] [Full Text]  
  • Russell, W. C. (2009). Adenoviruses: update on structure and function. J. Gen. Virol. 90: 1-20 [Abstract] [Full Text]  
  • Christensen, J. B., Byrd, S. A., Walker, A. K., Strahler, J. R., Andrews, P. C., Imperiale, M. J. (2008). Presence of the Adenovirus IVa2 Protein at a Single Vertex of the Mature Virion. J. Virol. 82: 9086-9093 [Abstract] [Full Text]  
  • Pantelic, R. S., Lockett, L. J., Rothnagel, R., Hankamer, B., Both, G. W. (2008). Cryoelectron Microscopy Map of Atadenovirus Reveals Cross-Genus Structural Differences from Human Adenovirus. J. Virol. 82: 7346-7356 [Abstract] [Full Text]  
  • Smith, J. G., Cassany, A., Gerace, L., Ralston, R., Nemerow, G. R. (2008). Neutralizing Antibody Blocks Adenovirus Infection by Arresting Microtubule-Dependent Cytoplasmic Transport. J. Virol. 82: 6492-6500 [Abstract] [Full Text]  
  • Kalyuzhniy, O., Di Paolo, N. C., Silvestry, M., Hofherr, S. E., Barry, M. A., Stewart, P. L., Shayakhmetov, D. M. (2008). Adenovirus serotype 5 hexon is critical for virus infection of hepatocytes in vivo. Proc. Natl. Acad. Sci. USA 105: 5483-5488 [Abstract] [Full Text]  
  • Schoehn, G., El Bakkouri, M., Fabry, C. M. S., Billet, O., Estrozi, L. F., Le, L., Curiel, D. T., Kajava, A. V., Ruigrok, R. W. H., Kremer, E. J. (2008). Three-Dimensional Structure of Canine Adenovirus Serotype 2 Capsid. J. Virol. 82: 3192-3203 [Abstract] [Full Text]  
  • Cottevieille, M., Larquet, E., Jonic, S., Petoukhov, M. V., Caprini, G., Paravisi, S., Svergun, D. I., Vanoni, M. A., Boisset, N. (2008). The Subnanometer Resolution Structure of the Glutamate Synthase 1.2-MDa Hexamer by Cryoelectron Microscopy and Its Oligomerization Behavior in Solution: FUNCTIONAL IMPLICATIONS. J. Biol. Chem. 283: 8237-8249 [Abstract] [Full Text]  
  • Guardado-Calvo, P., Llamas-Saiz, A. L., Fox, G. C., Langlois, P., van Raaij, M. J. (2007). Structure of the C-terminal head domain of the fowl adenovirus type 1 long fiber. J. Gen. Virol. 88: 2407-2416 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»