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 Zhang, X.
Right arrow Articles by Luo, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, X.
Right arrow Articles by Luo, M.

 Previous Article  |  Next Article 

Journal of Virology, January 2008, p. 674-682, Vol. 82, No. 2
0022-538X/08/$08.00+0     doi:10.1128/JVI.00935-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Role of Intermolecular Interactions of Vesicular Stomatitis Virus Nucleoprotein in RNA Encapsidation{triangledown}

Xin Zhang, Todd J. Green, Jun Tsao, Shihong Qiu, and Ming Luo*

Department of Microbiology, The University of Alabama at Birmingham, Birmingham, Alabama 35294

Received 1 May 2007/ Accepted 24 October 2007

The crystal structure of the vesicular stomatitis virus nucleoprotein (N) in complex with RNA reveals extensive and specific intermolecular interactions among the N molecules in the 10-member oligomer. What roles these interactions play in encapsidating RNA was studied by mutagenesis of the N protein. Three N mutants intended for disruption of the intermolecular interactions were designed and coexpressed with the phosphoprotein (P) in an Escherichia coli system previously described (T. J. Green et al., J. Virol. 74:9515-9524, 2000). Mutants N ({Delta}1-22), N ({Delta}347-352), and N (320-324, (Ala)5) lost RNA encapsidation and oligomerization but still bound with P. Another mutant, N (Ser290->Trp), was able to form a stable ring-like N oligomer and bind with the P protein but was no longer able to encapsidate RNA. The crystal structure of N (Ser290->Trp) at 2.8 Å resolution showed that this mutant can maintain all the same intermolecular interactions as the wild-type N except for a slight unwinding of the N-terminal lobe. These results suggest that the intermolecular contacts among the N molecules are required for encapsidation of the viral RNA.

* Corresponding author. Mailing address: Department of Microbiology, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35294. Phone: (205) 934-4259. Fax: (205) 975-9578. E-mail: mingluo{at}uab.edu

{triangledown} Published ahead of print on 14 November 2007.

Journal of Virology, January 2008, p. 674-682, Vol. 82, No. 2
0022-538X/08/$08.00+0     doi:10.1128/JVI.00935-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Nayak, D., Panda, D., Das, S. C., Luo, M., Pattnaik, A. K. (2009). Single-Amino-Acid Alterations in a Highly Conserved Central Region of Vesicular Stomatitis Virus N Protein Differentially Affect the Viral Nucleocapsid Template Functions. J. Virol. 83: 5525-5534 [Abstract] [Full Text]  
  • Huang, L., Massa, L., Karle, J. (2009). Kernel energy method applied to vesicular stomatitis virus nucleoprotein. Proc. Natl. Acad. Sci. USA 106: 1731-1736 [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»