A 3D Model of the Membrane Protein Complex Formed by the White Spot Syndrome Virus Structural Proteins

Chang, Ya‐Hsuan; Liu, Wang-Jing; Lee, Cheng-Chung; Chou, Tsung-Lu; Lee, Yuan-Ting; Wu, Tz-Shian; Huang, Jong Shin; Huang, Wei‐Tung; Lee, Tai-Lin; Kou, Guang Hsiung; Wang, Andrew H.‐J.; Lo, Chu Fang

doi:10.1371/journal.pone.0010718

Cited by 72 publications

(65 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Additionally, to increase the molecular mass of small ORFs (coding a product less than 10 kDa), such WSSV genes were cloned into pDHsp/EGFP-V5 vector (14) for fusion with an EGFP (enhanced green fluorescent protein) tag at the C-terminal end. The FLAG-tagged and V5-tagged WSSV fusion plasmids were cotransfected pairwise into Sf-9 (Spodoptera frugiperda) cells.…”

Section: Methodsmentioning

confidence: 99%

Construction and Application of a Protein Interaction Map for White Spot Syndrome Virus (WSSV)

Sangsuriya

Huang

Chu

et al. 2014

Molecular & Cellular Proteomics

Self Cite

View full text Add to dashboard Cite

Section: Methodsmentioning

confidence: 99%

Construction and Application of a Protein Interaction Map for White Spot Syndrome Virus (WSSV)

Sangsuriya

Huang

Chu

et al. 2014

Molecular & Cellular Proteomics

Self Cite

View full text Add to dashboard Cite

“…However, the location of VP24 on the WSSV membrane has been predicted differently in different models (24,27). In an early model, VP24 was proposed to be embedded in the WSSV envelope with only its C-terminal end projecting toward the inside the virion.…”

Section: Discussionmentioning

confidence: 99%

“…Among them, VP28, VP26, VP24, and VP19 are the four major viral envelope proteins (20, 21); these proteins form a multiprotein complex together with some low-abundance proteins (22)(23)(24)(25)(26). In addition to the importance of this envelope protein complex in virus assembly, it is thought to be an "infectome" that functions in cell recognition during infection (24,27). However, whether the viral envelope proteins play a role in the initial stage of WSSV invasion is unknown.…”

Section: Importancementioning

confidence: 99%

VP24 Is a Chitin-Binding Protein Involved in White Spot Syndrome Virus Infection

Han

et al. 2016

J Virol

View full text Add to dashboard Cite

Oral ingestion is the major route of infection for the white spot syndrome virus (WSSV). However, the mechanism by which virus particles in the digestive tract invade host cells is unknown. In the present study, we demonstrate that WSSV virions can bind to chitin through one of the major envelope proteins (VP24). Mutagenesis analysis indicated that amino acids (aa) 186 to 200 in the C terminus of VP24 were required for chitin binding. Moreover, the P-VP24 186 -200 peptide derived from the VP24 chitin binding region significantly inhibited the VP24-chitin interaction and the WSSV-chitin interaction, implying that VP24 participates in WSSV binding to chitin. Oral inoculation experiments showed that P-VP24 186 -200 treatment reduced the number of virus particles remaining in the digestive tract during the early stage of infection and greatly hindered WSSV proliferation in shrimp. These data indicate that binding of WSSV to chitin through the viral envelope protein VP24 is essential for WSSV per os infection and provide new ideas for preventing WSSV infection in shrimp farms. IMPORTANCEIn this study, we show that WSSV can bind to chitin through the envelope protein VP24. The chitin-binding domain of VP24 maps to amino acids 186 to 200 in the C terminus. Binding of WSSV to chitin through the viral envelope protein VP24 is essential for WSSV per os infection. These findings not only extend our knowledge of WSSV infection but also provide new insights into strategies to prevent WSSV infection in shrimp farms. W hite spot syndrome virus (WSSV) is an enveloped doublestranded DNA (dsDNA) virus belonging to the genus Whispovirus, family Nimaviridae (1). WSSV has caused enormous economic losses to the shrimp farming industry since 1993. Infectious WSSV virions are typically 250 to 380 nm in length and 120 to 150 nm in diameter (2, 3), and they contain a genome of ϳ300 kb that encodes ϳ180 proteins (4, 5).Ingestion of WSSV-infected sick or dead shrimp has been accepted as the major route of natural infection due to the cannibalistic nature of shrimp (6-11). Therefore the digestive tract of shrimp may be a primary site of infection. The digestive tract of shrimp is composed of the esophagus, stomach, midgut, and hindgut. The esophagus, stomach, and hindgut possess a chitinous lining, which is not present in the midgut (12, 13). Instead, the midgut epithelium is generally lined with the peritrophic membrane (PM), which is a noncellular structure surrounding the food bolus. The PM is composed of regularly arranged chitin fibrils embedded in a matrix of proteins, proteoglycans, and mucopolysaccharides (14-17). Therefore, WSSV must cross the PM in the midgut or the chitinous lining in the other parts of the digestive tract to traverse the basal membranes and reach the host cells. We speculate that the interaction between WSSV and chitin may be important for WSSV infection in the shrimp digestive tract.More than 40 WSSV structural proteins have been identified using proteomic methods to date (18)(19)(20). Among them, VP28,...

show abstract

“…Some WSSV envelope proteins involved in shrimp infection have been identified (54). For example, VP26 and VP28 anchored on the viral envelope membrane interact with the host cell membrane for effective transfer of the viral infection (50).…”

Section: Discussionmentioning

confidence: 99%

Prohibitin Interacts with Envelope Proteins of White Spot Syndrome Virus and Prevents Infection in the Red Swamp Crayfish, Procambarus clarkii

Lan

Sun

et al. 2013

J Virol

View full text Add to dashboard Cite

b Prohibitins (PHBs) are ubiquitously expressed conserved proteins in eukaryotes that are associated with apoptosis, cancer formation, aging, stress responses, cell proliferation, and immune regulation. However, the function of PHBs in crustacean immunity remains largely unknown. In the present study, we identified a PHB in Procambarus clarkii red swamp crayfish, which was designated PcPHB1. PcPHB1 was widely distributed in several tissues, and its expression was significantly upregulated by white spot syndrome virus (WSSV) challenge at the mRNA level and the protein level. These observations prompted us to investigate the role of PcPHB1 in the crayfish antiviral response. Recombinant PcPHB1 (rPcPHB1) significantly reduced the amount of WSSV in crayfish and the mortality of WSSV-infected crayfish. The quantity of WSSV in PcPHB1 knockdown crayfish was increased compared with that in the controls. The effects of RNA silencing were rescued by rPcPHB1 reinjection. We further confirmed the interaction of PcPHB1 with the WSSV envelope proteins VP28, VP26, and VP24 using pulldown and far-Western overlay assays. Finally, we observed that the colloidal gold-labeled PcPHB1 was located on the outer surface of the WSSV, which suggests that PcPHB1 specifically binds to the envelope proteins of WSSV. VP28, VP26, and VP24 are structural envelope proteins and are essential for attachment and entry into crayfish cells. Therefore, PcPHB1 exerts its anti-WSSV effect by binding to VP28, VP26, and VP24, preventing viral infection. This study is the first report on the antiviral function of PHB in the innate immune system of crustaceans.

show abstract

A 3D Model of the Membrane Protein Complex Formed by the White Spot Syndrome Virus Structural Proteins

Cited by 72 publications

References 50 publications

Construction and Application of a Protein Interaction Map for White Spot Syndrome Virus (WSSV)

Construction and Application of a Protein Interaction Map for White Spot Syndrome Virus (WSSV)

VP24 Is a Chitin-Binding Protein Involved in White Spot Syndrome Virus Infection

Prohibitin Interacts with Envelope Proteins of White Spot Syndrome Virus and Prevents Infection in the Red Swamp Crayfish, Procambarus clarkii

Contact Info

Product

Resources

About