VP292 of White spot syndrome virus Interacts with VP26

Li, Qian; Liu, Qinghui; Huang, Jie

doi:10.1007/s13337-012-0111-2

Cited by 6 publications

(4 citation statements)

References 18 publications

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“…This might explain the difference in the binding activities of the two AKs. VP26 was previously identified as an integral linker protein and can bind to host effector proteins to help transport virions into host cells (30,33,34). Previous studies found that viruses use host cell kinases for their replication, and arginine kinase has multiple functions in WSSV infection (21,35).…”

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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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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“…The VP41A envelope protein is known to interact with VP26, VP56 and VP28 envelope proteins [40,44] and with the viral envelope protein VP51A (VP52A for AF332093) [45]. It has been suggested that VP26 is anchored to the envelope with its N-terminal hydrophobic region, as a C-terminal region binds to the nucleocapsid [46], while VP51A is a type II transmembrane protein, with a transmembrane domain highly hydrophobic at its N-terminus and an exposed C-terminus on the virion surface [47].…”

Section: Discussionmentioning

confidence: 99%

In-Vivo Comparative Virulence of Different White Spot Syndrome Virus Isolates In Penaeus Vannamei And Whole Genome Comparison Analysis

Hernández-Montiel¹,

Weidmann

Bekaert

et al. 2021

Preprint

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White Spot Syndrome Virus (WSSV) infects several economically important aquacultural species, causing significant losses to the industry. This virus belongs to the Nimaviridae family, and has a dsDNA genome ranging from 257 to 309 kb (more than 20 isolate genomes fully sequenced and published to date). Multiple routes of infection could be the cause of the high virulence and mortality rates detected in shrimp species. In particular, Penaeus vannamei, differences in isolate virulence have been observed, along with controversy over whether deletions or insertions are associated with gain or loss of virulence.The pathogenicity of three isolates from three locations in Mexico (two from Sinaloa: 'CIAD', and 'Angostura', and one from Sonora: 'Sonora') was evaluated in vivo in white shrimp (P. vannamei) infection assays. Differences were observed in the mortality rate of shrimp among the three isolates, with the Sonora isolate being the most virulent. Subsequently, the complete WSSV genomes were sequenced in depth from the tissues of infected shrimp, and assembled in reference to the genome of isolate CN01 (KT995472), identifying genome sizes for Angostura and Sonora of 289,350 bp and 288,995 bp, respectively. Where three deletion zones were identified compared to CN01 comprising 15 genes, including three envelope proteins VP41A, VP52A and VP41B, one non-structural protein ICP35 and 11 others encoding proteins whose function is currently unknown. In addition, five genes (wsv129, wsv178, wsv204, wsv249 and wsv497) show a modified number of repeat motifs. The main implications and possible effects on viral infection of these modifications are discussed.

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“…The correct rLvRPL7 was expressed in E. coli Top10. The rLvRPL7 was confirmed by MS analysis and purified by affinity chromotography using a column of TALON Metal Affinity Resin as previously described [21].…”

Section: Recombinant Expression Of Lvrpl7 In Escherichia Colimentioning

confidence: 99%

White spot syndrome virus VP51 interact with ribosomal protein L7 of Litopenaeus vannamei

Liu

Guan

et al. 2015

Fish & Shellfish Immunology

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VP292 of White spot syndrome virus Interacts with VP26

Cited by 6 publications

References 18 publications

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

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

In-Vivo Comparative Virulence of Different White Spot Syndrome Virus Isolates In Penaeus Vannamei And Whole Genome Comparison Analysis

White spot syndrome virus VP51 interact with ribosomal protein L7 of Litopenaeus vannamei

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