SUMO and SUMO-Conjugating Enzyme E2 UBC9 Are Involved in White Spot Syndrome Virus Infection in Fenneropenaeus chinensis

Tang, Xiaoqian; Li, Wei; Xing, Jing; Sheng, Xiuzhen; Zhan, Wenbin

doi:10.1371/journal.pone.0150324

Cited by 5 publications

(4 citation statements)

References 33 publications

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“…Although the expression of SUMO has yet to be reported in the haemocytes of adult flies, Ubc9 (lesswright, Lwr) is specifically required in larval haemocytes for haematopoiesis [ 50 ], suggesting that SUMO is expressed in Drosophila haemocytes. SUMO and Ubc9 are also ubiquitously expressed in the shrimp species Fenneropenaeus chinensis [ 51 ], with high levels of expression in haemocytes and ovaries. Thus, the tissue expression profile of SUMO in arthropods seems to be conserved across evolution.…”

Section: Discussionmentioning

confidence: 99%

The SUMOylation pathway suppresses arbovirus replication in Aedes aegypti cells

et al. 2020

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Mosquitoes are responsible for the transmission of many clinically important arboviruses that cause significant levels of annual mortality and socioeconomic health burden worldwide. Deciphering the mechanisms by which mosquitoes modulate arbovirus infection is crucial to understand how viral-host interactions promote vector transmission and human disease. SUMOylation is a post-translational modification that leads to the covalent attachment of the Small Ubiquitin-like MOdifier (SUMO) protein to host factors, which in turn can modulate their stability, interaction networks, sub-cellular localisation, and biochemical function. While the SUMOylation pathway is known to play a key role in the regulation of host immune defences to virus infection in humans, the importance of this pathway during arbovirus infection in mosquito vectors, such as Aedes aegypti (Ae. aegypti), remains unknown. Here we characterise the sequence, structure, biochemical properties, and tissue-specific expression profiles of component proteins of the Ae. aegypti SUMOylation pathway. We demonstrate significant biochemical differences between Ae. aegypti and Homo sapiens SUMOylation pathways and identify cell-type specific patterns of SUMO expression in Ae. aegypti tissues known to support arbovirus replication. Importantly, depletion of core SUMOylation effector proteins (SUMO, Ubc9 and PIAS) in Ae. aegypti cells led to enhanced levels of arbovirus replication from three different families; Zika (Flaviviridae), Semliki Forest (Togaviridae), and Bunyamwera (Bunyaviridae) viruses. Our findings identify an important role for mosquito SUMOylation in the cellular restriction of arboviruses that may directly influence vector competence and transmission of clinically important arboviruses.

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Section: Discussionmentioning

confidence: 99%

The SUMOylation pathway suppresses arbovirus replication in Aedes aegypti cells

et al. 2020

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“…The ability of a pathogen to manipulate sumoylation processes and members of the sumoylation machinery is not unique to just viruses of vertebrates. Sumoylation processes are important for White spot syndrome virus (WSSV) infection in crustaceans [ 120 – 123 ], where infection increases levels of SUMO and Ubc9 at the mRNA and protein levels [ 121 , 122 ]. Silencing of SUMO and Ubc9 expression using RNA interference inhibits viral gene expression, viral replication, and shrimp mortality [ 122 ], which highlights the importance of sumoylation processes in the life cycle of WSSV.…”

Section: Introductionmentioning

confidence: 99%

“…Sumoylation processes are important for White spot syndrome virus (WSSV) infection in crustaceans [ 120 – 123 ], where infection increases levels of SUMO and Ubc9 at the mRNA and protein levels [ 121 , 122 ]. Silencing of SUMO and Ubc9 expression using RNA interference inhibits viral gene expression, viral replication, and shrimp mortality [ 122 ], which highlights the importance of sumoylation processes in the life cycle of WSSV. Another example is the geminivirus Rep protein [ 124 ], which binds to double-stranded DNA and catalyzes the cleavage and ligation of single-stranded DNA.…”

Section: Introductionmentioning

confidence: 99%

Viral manipulation of the cellular sumoylation machinery

2017

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Viruses exploit various cellular processes for their own benefit, including counteracting anti-viral responses and regulating viral replication and propagation. In the past 20 years, protein sumoylation has emerged as an important post-translational modification that is manipulated by viruses to modulate anti-viral responses, viral replication, and viral pathogenesis. The process of sumoylation is a multi-step cascade where a small ubiquitin-like modifier (SUMO) is covalently attached to a conserved ΨKxD/E motif within a target protein, altering the function of the modified protein. Here we review how viruses manipulate the cellular machinery at each step of the sumoylation process to favor viral survival and pathogenesis.

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“…Several host and viral proteins are known to be SUMOylated during viral infection. SUMOylation is not restricted to host cell proteins and is exploited to create conditions favorable to infection by many viruses including dengue virus [ 19 ], white spot syndrome virus infection in Fenneropenaeus chinensis [ 20 ], influenza A virus [ 21 ], hepatitis C virus [ 22 ], herpes simplex virus 1 [ 23 ] and Kaposi's sarcoma-associated herpes virus (KSHV) [ 24 ]. However, interaction between key viral proteins of any orthoreovirus and SUMOylation system remains unknown.…”

Section: Introductionmentioning

confidence: 99%

Orthoreovirus outer-fiber proteins are substrates for SUMO-conjugating enzyme Ubc9

Wang

et al. 2016

Oncotarget

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Reoviruses are potential anticancer agents due to their ability to induce cell death in tumor cells. Grass carp reovirus (GCRV) is one of the best characterized models on reovirus pathogenesis in vitro. However, there is little known about how SUMOylation affects reovirus pathogenesis. The SUMO conjugating enzyme 9 (Ubc9) determines the targets of SUMOylation. Here, the protein interactions between reovirus outer fiber proteins, specifically GCRV-104 VP55, and Ubc9 were probed using a yeast two-hybrid system. The N-terminal coiled-coil domain of VP55, containing a single lysine residue, was responsible for the interaction between VP55 and Ubc9 in yeast. In solid phase binding assays, a single amino acid mutation (K87R) prevented Ubc9 from binding to VP55. Overexpression of Ubc9 enhanced GCRV-104 infection efficiency, and knockdown of Ubc9 in CIK cells inhibited viral replication, which suggested that Ubc9 was a proviral factor. Furthermore, Ubc9 was shown to bind outer fiber proteins from type II GCRV, avian reovirus and mammalian reovirus in yeast. To our knowledge, this is the first study to show that Ubc9 binds to reovirus outer-fiber proteins and likely contributes to efficient orthoreovirus replication. These results suggest that SUMOylation modifications could be targeted to improve the therapeutic efficacy of oncolytic reovirus.

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SUMO and SUMO-Conjugating Enzyme E2 UBC9 Are Involved in White Spot Syndrome Virus Infection in Fenneropenaeus chinensis

Cited by 5 publications

References 33 publications

The SUMOylation pathway suppresses arbovirus replication in Aedes aegypti cells

The SUMOylation pathway suppresses arbovirus replication in Aedes aegypti cells

Viral manipulation of the cellular sumoylation machinery

Orthoreovirus outer-fiber proteins are substrates for SUMO-conjugating enzyme Ubc9

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