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 Dong, X. F.
Right arrow Articles by Schneemann, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dong, X. F.
Right arrow Articles by Schneemann, A.

 Previous Article  |  Next Article 

J Virol, July 1998, p. 6024-6033, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Particle Polymorphism Caused by Deletion of a Peptide Molecular Switch in a Quasiequivalent Icosahedral Virusdagger

X. Fan Dong,1 Padmaja Natarajan,1 Mariana Tihova,2 John E. Johnson,1 and Anette Schneemann1,*

Department of Molecular Biology1 and Department of Cell Biology,2 The Scripps Research Institute, La Jolla, California 92037

Received 10 February 1998/Accepted 9 April 1998

The capsid of flock house virus is composed of 180 copies of a single type of coat protein which forms a T=3 icosahedral shell. High-resolution structural analysis has shown that the protein subunits, although chemically identical, form different contacts across the twofold axes of the virus particle. Subunits that are related by icosahedral twofold symmetry form flat contacts, whereas subunits that are related by quasi-twofold symmetry form bent contacts. The flat contacts are due to the presence of ordered genomic RNA and an ordered peptide arm which is inserted in the groove between the subunits and prevents them from forming the dihedral angle observed at the bent quasi-twofold contacts. We hypothesized that by deleting the residues that constitute the ordered peptide arm, formation of flat contacts should be impossible and therefore result in assembly of particles with only bent contacts. Such particles would have T=1 symmetry. To test this hypothesis we generated two deletion mutants in which either 50 or 31 residues were eliminated from the N terminus of the coat protein. We found that in the absence of residues 1 to 50, assembly was completely inhibited, presumably because the mutation removed a cluster of positively charged amino acids required for neutralization of encapsidated RNA. When the deletion was restricted to residues 1 to 31, assembly occurred, but the products were highly heterogeneous. Small bacilliform-like structures and irregular structures as well as wild-type-like T=3 particles were detected. The anticipated T=1 particles, on the other hand, were not observed. We conclude that residues 20 to 30 are not critical for formation of flat protein contacts and formation of T=3 particles. However, the N terminus of the coat protein appears to play an essential role in regulating assembly such that only one product, T=3 particles, is synthesized.

* Corresponding author. Mailing address: Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037. Phone: (619) 784-8643. Fax: (619) 784-8660. E-mail: aschneem{at}scripps.edu.

dagger Manuscript no. 11439MB from The Scripps Research Institute.

J Virol, July 1998, p. 6024-6033, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Venter, P. A., Marshall, D., Schneemann, A. (2009). Dual Roles for an Arginine-Rich Motif in Specific Genome Recognition and Localization of Viral Coat Protein to RNA Replication Sites in Flock House Virus-Infected Cells. J. Virol. 83: 2872-2882 [Abstract] [Full Text]  
  • Annamalai, P., Rofail, F., DeMason, D. A., Rao, A. L. N. (2008). Replication-Coupled Packaging Mechanism in Positive-Strand RNA Viruses: Synchronized Coexpression of Functional Multigenome RNA Components of an Animal and a Plant Virus in Nicotiana benthamiana Cells by Agroinfiltration. J. Virol. 82: 1484-1495 [Abstract] [Full Text]  
  • Kakani, K., Reade, R., Katpally, U., Smith, T., Rochon, D. (2008). Induction of Particle Polymorphism by Cucumber Necrosis Virus Coat Protein Mutants In Vivo. J. Virol. 82: 1547-1557 [Abstract] [Full Text]  
  • Tomasicchio, M., Venter, P. A., H. J. Gordon, K., N. Hanzlik, T., Dorrington, R. A. (2007). Induction of apoptosis in Saccharomyces cerevisiae results in the spontaneous maturation of tetravirus procapsids in vivo. J. Gen. Virol. 88: 1576-1582 [Abstract] [Full Text]  
  • Venter, P. A., Schneemann, A. (2007). Assembly of Two Independent Populations of Flock House Virus Particles with Distinct RNA Packaging Characteristics in the Same Cell. J. Virol. 81: 613-619 [Abstract] [Full Text]  
  • Belyi, V. A., Muthukumar, M. (2006). Electrostatic origin of the genome packing in viruses. Proc. Natl. Acad. Sci. USA 103: 17174-17178 [Abstract] [Full Text]  
  • Hui, E., Rochon, D. (2006). Evaluation of the Roles of Specific Regions of the Cucumber Necrosis Virus Coat Protein Arm in Particle Accumulation and Fungus Transmission.. J. Virol. 80: 5968-5975 [Abstract] [Full Text]  
  • Wang, X.-H., Aliyari, R., Li, W.-X., Li, H.-W., Kim, K., Carthew, R., Atkinson, P., Ding, S.-W. (2006). RNA Interference Directs Innate Immunity Against Viruses in Adult Drosophila. Science 312: 452-454 [Abstract] [Full Text]  
  • Venter, P. A., Krishna, N. K., Schneemann, A. (2005). Capsid Protein Synthesis from Replicating RNA Directs Specific Packaging of the Genome of a Multipartite, Positive-Strand RNA Virus. J. Virol. 79: 6239-6248 [Abstract] [Full Text]  
  • Reguera, J., Grueso, E., Carreira, A., Sanchez-Martinez, C., Almendral, J. M., Mateu, M. G. (2005). Functional Relevance of Amino Acid Residues Involved in Interactions with Ordered Nucleic Acid in a Spherical Virus. J. Biol. Chem. 280: 17969-17977 [Abstract] [Full Text]  
  • Zandi, R., Reguera, D., Bruinsma, R. F., Gelbart, W. M., Rudnick, J. (2004). From The Cover: Origin of icosahedral symmetry in viruses. Proc. Natl. Acad. Sci. USA 101: 15556-15560 [Abstract] [Full Text]  
  • Lee, K. K., Tang, J., Taylor, D., Bothner, B., Johnson, J. E. (2004). Small Compounds Targeted to Subunit Interfaces Arrest Maturation in a Nonenveloped, Icosahedral Animal Virus. J. Virol. 78: 7208-7216 [Abstract] [Full Text]  
  • Tihova, M., Dryden, K. A., Le, T.-v. L., Harvey, S. C., Johnson, J. E., Yeager, M., Schneemann, A. (2004). Nodavirus Coat Protein Imposes Dodecahedral RNA Structure Independent of Nucleotide Sequence and Length. J. Virol. 78: 2897-2905 [Abstract] [Full Text]  
  • Johnson, K. N., Ball, L. A. (2003). Virions of Pariacoto virus contain a minor protein translated from the second AUG codon of the capsid protein open reading frame. J. Gen. Virol. 84: 2847-2852 [Abstract] [Full Text]  
  • Lu, M.-W., Liu, W., Lin, C.-S. (2003). Infection competition against grouper nervous necrosis virus by virus-like particles produced in Escherichia coli. J. Gen. Virol. 84: 1577-1582 [Abstract] [Full Text]  
  • Taylor, D. J., Krishna, N. K., Canady, M. A., Schneemann, A., Johnson, J. E. (2002). Large-Scale, pH-Dependent, Quaternary Structure Changes in an RNA Virus Capsid Are Reversible in the Absence of Subunit Autoproteolysis. J. Virol. 76: 9972-9980 [Abstract] [Full Text]  
  • Hafenstein, S., Fane, B. A. (2002). {phi}X174 Genome-Capsid Interactions Influence the Biophysical Properties of the Virion: Evidence for a Scaffolding-Like Function for the Genome during the Final Stages of Morphogenesis. J. Virol. 76: 5350-5356 [Abstract] [Full Text]  
  • Bertolotti-Ciarlet, A., White, L. J., Chen, R., Prasad, B. V. V., Estes, M. K. (2002). Structural Requirements for the Assembly of Norwalk Virus-Like Particles. J. Virol. 76: 4044-4055 [Abstract] [Full Text]  
  • Johnson, K. N., Ball, L. A. (2001). Recovery of Infectious Pariacoto Virus from cDNA Clones and Identification of Susceptible Cell Lines. J. Virol. 75: 12220-12227 [Abstract] [Full Text]  
  • Schneemann, A., Marshall, D. (1998). Specific Encapsidation of Nodavirus RNAs Is Mediated through the C Terminus of Capsid Precursor Protein Alpha. J. Virol. 72: 8738-8746 [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»