This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Kronenberg, S.
Right arrow Articles by Kleinschmidt, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kronenberg, S.
Right arrow Articles by Kleinschmidt, J. A.

 Previous Article  |  Next Article 

Journal of Virology, May 2005, p. 5296-5303, Vol. 79, No. 9
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.9.5296-5303.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Conformational Change in the Adeno-Associated Virus Type 2 Capsid Leads to the Exposure of Hidden VP1 N Termini

Stephanie Kronenberg,1,2,{dagger} Bettina Böttcher, Claus W. von der Lieth,3 Svenja Bleker,1 and Jürgen A. Kleinschmidt1*

German Cancer Research Centre, Tumor Virology,1 Central Spectroscopy,2 European Molecular Biology Laboratory Heidelberg, Structural and Computational Biology Programme, Heidelberg, Germany3

Received 20 September 2004/ Accepted 16 December 2004

The complex infection process of parvoviruses is not well understood so far. An important role has been attributed to a phospholipase A2 domain which is located within the unique N terminus of the capsid protein VP1. Based on the structural difference between adeno-associated virus type 2 wild-type capsids and capsids lacking VP1 or VP2, we show via electron cryomicroscopy that the N termini of VP1 and VP2 are involved in forming globules inside the capsids of empty and full particles. Upon limited heat shock, VP1 and possibly VP2 become exposed on the outsides of full but not empty capsids, which is correlated with the disappearance of the globules in the inner surfaces of the capsids. Using molecular modeling, we discuss the constraints on the release of the globularly organized VP1-unique N termini through the channels at the fivefold symmetry axes outside of the capsid.

* Corresponding author. Mailing address: Applied Tumor Virology, German Cancer Research Centre, Im Neuenheimer Feld 242, 69120 Heidelberg, Germany. Phone: 49 6221 424978. Fax: 49 6221 424962. E-mail: J.Kleinschmidt{at}DKFZ-Heidelberg.de.

{dagger} S.K. and B.B. contributed equally to this work.

Journal of Virology, May 2005, p. 5296-5303, Vol. 79, No. 9
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.9.5296-5303.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Johnson, J. S., Samulski, R. J. (2009). Enhancement of Adeno-Associated Virus Infection by Mobilizing Capsids into and Out of the Nucleolus. J. Virol. 83: 2632-2644 [Abstract] [Full Text]  
  • Bonsch, C., Kempf, C., Ros, C. (2008). Interaction of Parvovirus B19 with Human Erythrocytes Alters Virus Structure and Cell Membrane Integrity. J. Virol. 82: 11784-11791 [Abstract] [Full Text]  
  • Kittelmann, K., Jeske, H. (2008). Disassembly of African cassava mosaic virus. J. Gen. Virol. 89: 2029-2036 [Abstract] [Full Text]  
  • Kaufmann, B., Chipman, P. R., Kostyuchenko, V. A., Modrow, S., Rossmann, M. G. (2008). Visualization of the Externalized VP2 N Termini of Infectious Human Parvovirus B19. J. Virol. 82: 7306-7312 [Abstract] [Full Text]  
  • Grimm, D., Lee, J. S., Wang, L., Desai, T., Akache, B., Storm, T. A., Kay, M. A. (2008). In Vitro and In Vivo Gene Therapy Vector Evolution via Multispecies Interbreeding and Retargeting of Adeno-Associated Viruses. J. Virol. 82: 5887-5911 [Abstract] [Full Text]  
  • DiPrimio, N., Asokan, A., Govindasamy, L., Agbandje-McKenna, M., Samulski, R. J. (2008). Surface Loop Dynamics in Adeno-Associated Virus Capsid Assembly. J. Virol. 82: 5178-5189 [Abstract] [Full Text]  
  • Nam, H.-J., Lane, M. D., Padron, E., Gurda, B., McKenna, R., Kohlbrenner, E., Aslanidi, G., Byrne, B., Muzyczka, N., Zolotukhin, S., Agbandje-McKenna, M. (2007). Structure of Adeno-Associated Virus Serotype 8, a Gene Therapy Vector. J. Virol. 81: 12260-12271 [Abstract] [Full Text]  
  • Ward, P., Clement, N., Linden, R. M. (2007). cis Effects in Adeno-Associated Virus Type 2 Replication. J. Virol. 81: 9976-9989 [Abstract] [Full Text]  
  • Grieger, J. C., Johnson, J. S., Gurda-Whitaker, B., Agbandje-McKenna, M., Samulski, R. J. (2007). Surface-Exposed Adeno-Associated Virus Vp1-NLS Capsid Fusion Protein Rescues Infectivity of Noninfectious Wild-Type Vp2/Vp3 and Vp3-Only Capsids but Not That of Fivefold Pore Mutant Virions. J. Virol. 81: 7833-7843 [Abstract] [Full Text]  
  • Ros, C., Gerber, M., Kempf, C. (2006). Conformational Changes in the VP1-Unique Region of Native Human Parvovirus B19 Lead to Exposure of Internal Sequences That Play a Role in Virus Neutralization and Infectivity. J. Virol. 80: 12017-12024 [Abstract] [Full Text]  
  • Govindasamy, L., Padron, E., McKenna, R., Muzyczka, N., Kaludov, N., Chiorini, J. A., Agbandje-McKenna, M. (2006). Structurally Mapping the Diverse Phenotype of Adeno-Associated Virus Serotype 4. J. Virol. 80: 11556-11570 [Abstract] [Full Text]  
  • Sonntag, F., Bleker, S., Leuchs, B., Fischer, R., Kleinschmidt, J. A. (2006). Adeno-Associated Virus Type 2 Capsids with Externalized VP1/VP2 Trafficking Domains Are Generated prior to Passage through the Cytoplasm and Are Maintained until Uncoating Occurs in the Nucleus. J. Virol. 80: 11040-11054 [Abstract] [Full Text]  
  • Grieger, J. C., Snowdy, S., Samulski, R. J. (2006). Separate Basic Region Motifs within the Adeno-Associated Virus Capsid Proteins Are Essential for Infectivity and Assembly.. J. Virol. 80: 5199-5210 [Abstract] [Full Text]  
  • Murray, S., Nilsson, C. L., Hare, J. T., Emmett, M. R., Korostelev, A., Ongley, H., Marshall, A. G., Chapman, M. S. (2006). Characterization of the Capsid Protein Glycosylation of Adeno-Associated Virus Type 2 by High-Resolution Mass Spectrometry.. J. Virol. 80: 6171-6176 [Abstract] [Full Text]  
  • Urabe, M., Nakakura, T., Xin, K.-Q., Obara, Y., Mizukami, H., Kume, A., Kotin, R. M., Ozawa, K. (2006). Scalable Generation of High-Titer Recombinant Adeno-Associated Virus Type 5 in Insect Cells. J. Virol. 80: 1874-1885 [Abstract] [Full Text]  
  • Bleker, S., Pawlita, M., Kleinschmidt, J. A. (2006). Impact of Capsid Conformation and Rep-Capsid Interactions on Adeno-Associated Virus Type 2 Genome Packaging. J. Virol. 80: 810-820 [Abstract] [Full Text]  
  • Lochrie, M. A., Tatsuno, G. P., Christie, B., McDonnell, J. W., Zhou, S., Surosky, R., Pierce, G. F., Colosi, P. (2006). Mutations on the External Surfaces of Adeno-Associated Virus Type 2 Capsids That Affect Transduction and Neutralization. J. Virol. 80: 821-834 [Abstract] [Full Text]  
  • Mani, B., Baltzer, C., Valle, N., Almendral, J. M., Kempf, C., Ros, C. (2006). Low pH-Dependent Endosomal Processing of the Incoming Parvovirus Minute Virus of Mice Virion Leads to Externalization of the VP1 N-Terminal Sequence (N-VP1), N-VP2 Cleavage, and Uncoating of the Full-Length Genome. J. Virol. 80: 1015-1024 [Abstract] [Full Text]  
  • Farr, G. A., Cotmore, S. F., Tattersall, P. (2006). VP2 Cleavage and the Leucine Ring at the Base of the Fivefold Cylinder Control pH-Dependent Externalization of both the VP1 N Terminus and the Genome of Minute Virus of Mice. J. Virol. 80: 161-171 [Abstract] [Full Text]  
  • Grimm, D., Pandey, K., Nakai, H., Storm, T. A., Kay, M. A. (2006). Liver Transduction with Recombinant Adeno-Associated Virus Is Primarily Restricted by Capsid Serotype Not Vector Genotype. J. Virol. 80: 426-439 [Abstract] [Full Text]  
  • Lux, K., Goerlitz, N., Schlemminger, S., Perabo, L., Goldnau, D., Endell, J., Leike, K., Kofler, D. M., Finke, S., Hallek, M., Buning, H. (2005). Green Fluorescent Protein-Tagged Adeno-Associated Virus Particles Allow the Study of Cytosolic and Nuclear Trafficking. J. Virol. 79: 11776-11787 [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»