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Published on: October 21, 2014
Crystal structures of major envelope proteins VP26 and VP28 from white spot syndrome virus shed light on their
Xuhua Tang1, Jinlu Wu, J Sivaraman
1Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Republic of Singapore.
Abstract:
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 A, 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 beta-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 beta-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.
Insights
Structural analysis of White spot syndrome virus (WSSV) envelope proteins VP26 and VP28 reveals their beta-barrel structure and surface localization, crucial for host interaction and potential drug development.
Area of Science:
- Virology
- Structural Biology
- Crustacean Pathology
Background:
- White spot syndrome virus (WSSV) is a significant pathogen affecting crustaceans.
- Viral envelope proteins are critical for initiating host interaction and infection.
- Understanding WSSV envelope protein structure is key to developing countermeasures.
Purpose of the Study:
- To determine the crystal structures of WSSV envelope proteins VP26 and VP28.
- To investigate the localization of VP26 and VP28 on the WSSV envelope.
- To explore the evolutionary relationships and functional implications of these proteins.
Main Methods:
- X-ray crystallography was used to resolve the structures of VP26 and VP28 at 2.2 and 2.0 Å, respectively.
- Immunoelectron microscopy was employed to determine the localization of these proteins.
- Structural comparisons were made with other viral proteins.
Main Results:
- The crystal structures of VP26 and VP28 were determined, revealing a beta-barrel architecture.
- VP26 and VP28 were localized to the outer surface of the WSSV envelope, forming protrusions.
- Structural similarities suggest evolutionary links between WSSV proteins and those of other viruses.
Conclusions:
- VP26 and VP28 are major structural components of the WSSV envelope, likely involved in host interaction.
- The protruding beta-barrel domains may mediate host receptor binding or membrane fusion.
- These findings provide a basis for developing novel antiviral drugs and vaccines against WSSV.
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