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Journal of Virology, June 2007, p. 6709-6717, Vol. 81, No. 12
0022-538X/07/$08.00+0     doi:10.1128/JVI.02505-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Crystal Structures of Major Envelope Proteins VP26 and VP28 from White Spot Syndrome Virus Shed Light on Their Evolutionary Relationship{triangledown}

Xuhua Tang, Jinlu Wu, J. Sivaraman,* and Choy Leong Hew*

Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Republic of Singapore

Received 14 November 2006/ Accepted 27 March 2007

White spot syndrome virus (WSSV) is a virulent pathogen known to infect various crustaceans. It has bacilliform morphology with a tail-like appendage at one end. The envelope consists of four major proteins. Envelope structural proteins play a crucial role in viral infection and are believed to be the first molecules to interact with the host. Here, we report the localization and crystal structure of major envelope proteins VP26 and VP28 from WSSV at resolutions of 2.2 and 2.0 Å, respectively. These two proteins alone account for approximately 60% of the envelope, and their structures represent the first two structural envelope proteins of WSSV. Structural comparisons among VP26, VP28, and other viral proteins reveal an evolutionary relationship between WSSV envelope proteins and structural proteins from other viruses. Both proteins adopt ß-barrel architecture with a protruding N-terminal region. We have investigated the localization of VP26 and VP28 using immunoelectron microscopy. This study suggests that VP26 and VP28 are located on the outer surface of the virus and are observed as a surface protrusion in the WSSV envelope, and this is the first convincing observation for VP26. Based on our studies combined with the literature, we speculate that the predicted N-terminal transmembrane region of VP26 and VP28 may anchor on the viral envelope membrane, making the core ß-barrel protrude outside the envelope, possibly to interact with the host receptor or to fuse with the host cell membrane for effective transfer of the viral infection. Furthermore, it is tempting to extend this host interaction mode to other structural viral proteins of similar structures. Our finding has the potential to extend further toward drug and vaccine development against WSSV.

* Corresponding author. Mailing address: Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Republic of Singapore. Phone: 65 6516 2692. Fax: 65 6779 5671. E-mail for Choy Leong Hew: dbshewcl{at}nus.edu.sg. E-mail for J. Sivaraman: dbsjayar{at}nus.edu.sg

{triangledown} Published ahead of print on 4 April 2007.

Journal of Virology, June 2007, p. 6709-6717, Vol. 81, No. 12
0022-538X/07/$08.00+0     doi:10.1128/JVI.02505-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zhou, Q., Xu, L., Li, H., Qi, Y.-P., Yang, F. (2009). Four Major Envelope Proteins of White Spot Syndrome Virus Bind To Form a Complex. J. Virol. 83: 4709-4712 [Abstract] [Full Text]  
  • Chang, Y.-S., Liu, W.-J., Chou, T.-L., Lee, Y.-T., Lee, T.-L., Huang, W.-T., Kou, G.-H., Lo, C.-F. (2008). Characterization of White Spot Syndrome Virus Envelope Protein VP51A and Its Interaction with Viral Tegument Protein VP26. J. Virol. 82: 12555-12564 [Abstract] [Full Text]  
  • Wan, Q., Xu, L., Yang, F. (2008). VP26 of White Spot Syndrome Virus Functions as a Linker Protein between the Envelope and Nucleocapsid of Virions by Binding with VP51. J. Virol. 82: 12598-12601 [Abstract] [Full Text]  
  • Wu, J., Lin, Q., Lim, T. K., Liu, T., Hew, C.-L. (2007). White Spot Syndrome Virus Proteins and Differentially Expressed Host Proteins Identified in Shrimp Epithelium by Shotgun Proteomics and Cleavable Isotope-Coded Affinity Tag. J. Virol. 81: 11681-11689 [Abstract] [Full Text]  


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