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

Lan, Jiang-Feng; Li, Xin-Cang; Sun, Jiejie; Gong, Jing; Wang, Xianwei; Shi, Xiaoping; Shi, Li-Jie; Weng, Yuding; Zhao, Xiao‐Fan; Wang, Jinxing

doi:10.1128/jvi.02198-13

Cited by 50 publications

(28 citation statements)

References 55 publications

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“…VP19, VP24, VP26 and VP28 are the four major envelope proteins of WSSV and function in virus entry and systemic infection [38–40]. VP24, VP26 and VP28 share high sequence homology with each other; however, VP19 has a unique structure and biological character [41, 42]. The CCP domain exists mainly in complement system proteins and promotes the formation of oligomers [43].…”

Section: Discussionmentioning

confidence: 99%

Scavenger Receptor C Mediates Phagocytosis of White Spot Syndrome Virus and Restricts Virus Proliferation in Shrimp

et al. 2016

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Scavenger receptors are an important class of pattern recognition receptors that play several important roles in host defense against pathogens. The class C scavenger receptors (SRCs) have only been identified in a few invertebrates, and their role in the immune response against viruses is seldom studied. In this study, we firstly identified an SRC from kuruma shrimp, Marsupenaeus japonicus, designated MjSRC, which was significantly upregulated after white spot syndrome virus (WSSV) challenge at the mRNA and protein levels in hemocytes. The quantity of WSSV increased in shrimp after knockdown of MjSRC, compared with the controls. Furthermore, overexpression of MjSRC led to enhanced WSSV elimination via phagocytosis by hemocytes. Pull-down and co-immunoprecipitation assays demonstrated the interaction between MjSRC and the WSSV envelope protein. Electron microscopy observation indicated that the colloidal gold-labeled extracellular domain of MjSRC was located on the outer surface of WSSV. MjSRC formed a trimer and was internalized into the cytoplasm after WSSV challenge, and the internalization was strongly inhibited after knockdown of Mjβ-arrestin2. Further studies found that Mjβ-arrestin2 interacted with the intracellular domain of MjSRC and induced the internalization of WSSV in a clathrin-dependent manner. WSSV were co-localized with lysosomes in hemocytes and the WSSV quantity in shrimp increased after injection of lysosome inhibitor, chloroquine. Collectively, this study demonstrated that MjSRC recognized WSSV via its extracellular domain and invoked hemocyte phagocytosis to restrict WSSV systemic infection. This is the first study to report an SRC as a pattern recognition receptor promoting phagocytosis of a virus.

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Section: Discussionmentioning

confidence: 99%

Scavenger Receptor C Mediates Phagocytosis of White Spot Syndrome Virus and Restricts Virus Proliferation in Shrimp

et al. 2016

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“…The principle envelope proteins of WSSV, viral protein 28 (VP28) and VP19, play important roles in virus entry and systemic infection (9,10). Although some molecules from crustaceans were shown to be involved in virus infection or antiviral responses (11)(12)(13)(14), how WSSV is recognized by the host and how the virions enter the cells remain largely unknown. Thus, identification of critical factors during WSSV infection, especially the early viral entry stage, would be of great help in understanding the virus-host interaction and discovering the targets for disease control and prevention.…”

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confidence: 99%

Collaboration between a Soluble C-Type Lectin and Calreticulin Facilitates White Spot Syndrome Virus Infection in Shrimp

Wang

et al. 2014

The Journal of Immunology

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White spot syndrome virus (WSSV) mainly infects crustaceans through the digestive tract. Whether C-type lectins (CLs), which are important receptors for many viruses, participate in WSSV infection in the shrimp stomach remains unknown. In this study, we orally infected kuruma shrimp Marsupenaeus japonicus to model the natural transmission of WSSV and identified a CL (designated as M. japonicus stomach virus–associated CL [MjsvCL]) that was significantly induced by virus infection in the stomach. Knockdown of MjsvCL expression by RNA interference suppressed the virus replication, whereas exogenous MjsvCL enhanced it. Further analysis by GST pull-down and coimmunoprecipitation showed that MjsvCL could bind to viral protein 28, the most abundant and functionally relevant envelope protein of WSSV. Furthermore, cell-surface calreticulin was identified as a receptor of MjsvCL, and the interaction between these proteins was a determinant for the viral infection–promoting activity of MjsvCL. The MjsvCL–calreticulin pathway facilitated virus entry likely in a cholesterol-dependent manner. This study provides insights into a mechanism by which soluble CLs capture and present virions to the cell-surface receptor to facilitate viral infection.

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“…Further study found that Litopenaeus vannamei AK (LvAK) interacted with VP14 in WSSV-infected shrimp and was beneficial for WSSV proliferation (21). Structural envelope proteins of viruses, which are the first components to come into contact with host cells (30), have been reported to have crucial roles in the entrance of viruses into host cells (31,32). VP19, VP24, VP26, and VP28 are the four major WSSV structural proteins and have been found to play key roles in WSSV infection (32).…”

Section: Discussionmentioning

confidence: 99%

“…Structural envelope proteins of viruses, which are the first components to come into contact with host cells (30), have been reported to have crucial roles in the entrance of viruses into host cells (31,32). VP19, VP24, VP26, and VP28 are the four major WSSV structural proteins and have been found to play key roles in WSSV infection (32). Therefore, we performed pulldown assays of MjAK with these WSSV envelope proteins and found that MjAK interacts with WSSV VP26 but not with VP14.…”

Section: Discussionmentioning

confidence: 99%

Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp

Jiang

Wei

et al. 2017

J Virol

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Many types of small GTPases are widely expressed in eukaryotes and have different functions. As a crucial member of the Rho GTPase family, Cdc42 serves a number of functions, such as regulating cell growth, migration, and cell movement. Several RNA viruses employ Cdc42-hijacking tactics in their target cell entry processes. However, the function of Cdc42 in shrimp antiviral immunity is not clear. In this study, we identified a Cdc42 protein in the kuruma shrimp (Marsupenaeus japonicus) and named it MjCdc42. MjCdc42 was upregulated in shrimp challenged by white spot syndrome virus (WSSV). The knockdown of MjCdc42 and injection of Cdc42 inhibitors increased the proliferation of WSSV. Further experiments determined that MjCdc42 interacted with an arginine kinase (MjAK). By analyzing the binding activity and enzyme activity of MjAK and its mutant, ΔMjAK, we found that MjAK could enhance the replication of WSSV in shrimp. MjAK interacted with the envelope protein VP26 of WSSV. An inhibitor of AK activity, quercetin, could impair the function of MjAK in WSSV replication. Further study demonstrated that the binding of MjCdc42 and MjAK depends on Cys 271 of MjAK and suppresses the WSSV replication-promoting effect of MjAK. By interacting with the active site of MjAK and suppressing its enzyme activity, MjCdc42 inhibits WSSV replication in shrimp. Our results demonstrate a new function of Cdc42 in the cellular defense against viral infection in addition to the regulation of actin and phagocytosis, which has been reported in previous studies. IMPORTANCEThe interaction of Cdc42 with arginine kinase plays a crucial role in the host defense against WSSV infection. This study identifies a new mechanism of Cdc42 in innate immunity and enriches the knowledge of the antiviral innate immunity of invertebrates.

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

Cited by 50 publications

References 55 publications

Scavenger Receptor C Mediates Phagocytosis of White Spot Syndrome Virus and Restricts Virus Proliferation in Shrimp

Scavenger Receptor C Mediates Phagocytosis of White Spot Syndrome Virus and Restricts Virus Proliferation in Shrimp

Collaboration between a Soluble C-Type Lectin and Calreticulin Facilitates White Spot Syndrome Virus Infection in Shrimp

Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp

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