PDBsum entry 2edm

Viral protein

PDB id: 2edm

Contents

Protein chain

161 a.a.

Waters ×153

PDB id:

2edm

Name:

Viral protein

Title:

Crystal structure of envelope protein vp26 from white spot syndrome virus (wssv)

Structure:

22kda structural protein vp22. Chain: a. Fragment: residues 41-201. Synonym: vp26, vp26 structural protein, wssv367, major virion protein vp26, orf153, vp26, gene family 1, wsv311, p22, 26 kda structural protein vp26. Engineered: yes

Source:

Shrimp white spot syndrome virus. Organism_taxid: 92652. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.20Å R-factor: 0.217 R-free: 0.278

Authors:

C.L.Hew,X.H.Tang,J.Sivaraman

Key ref:

X.Tang et al. (2007). Crystal structures of major envelope proteins VP26 and VP28 from white spot syndrome virus shed light on their evolutionary relationship. J Virol, 81, 6709-6717. PubMed id: 17409146

Date:

14-Feb-07 Release date: 05-Jun-07

Protein chain

Q0PW17  (Q0PW17_WSSV) -  VP26 (Fragment) from White spot syndrome virus

Seq: 204 a.a.

Struc: 161 a.a.

Enzyme reactions

• Enzyme class: E.C.?

J Virol 81:6709-6717 (2007)

PubMed id: 17409146

Crystal structures of major envelope proteins VP26 and VP28 from white spot syndrome virus shed light on their evolutionary relationship.

X.Tang, J.Wu, J.Sivaraman, C.L.Hew.

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.