The immediate early protein WSV187 can influence viral replication via regulation of JAK/STAT pathway in Drosophila

Pan, Changkun; Wang, Wei; Yuan, Huifang; Yang, Lirong; Chen, Baoru; Li, Dengfeng; Chen, Jianming

doi:10.1016/j.dci.2017.02.012

Cited by 7 publications

(4 citation statements)

References 55 publications

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“…WSSV can regulate host immunity and take advantage of miR-S5 to regulate hemocyte phagocytosis and apoptosis [36]. Wsv187, which is encoded by the WSSV immediate early gene, activates the host's JAK/ STAT pathway for replication [37]. Additionally, wsv249 encodes an E3 ubiquitin ligase that can mediate the ubiquitination of host immune effect molecules.…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of a novel L-type lectin (MjLTL2) from kuruma shrimp (Marsupenaeus japonicus)

Jing

Liu

et al. 2020

Fish & Shellfish Immunology

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L-type lectins (LTLs) belong to the lectin family and are characterized by a conserved structural motif in their carbohydrate recognition domain. LTLs are homologous to leguminous lectins. In this study, we identified and functionally characterized an LTL from kuruma shrimp Marsupenaeus japonicus. We designated this LTL as MjLTL2. MjLTL2 contains a signal peptide, a Lectin_leg domain, a coiled coil, and transmembrane domain. MjLTL2 is distributed in hemocytes, heart, hepatopancreas, gill, stomach, and intestine; higher expression levels are seen in hemocytes and the hepatopancreas than in other tissues. MjLTL2 was upregulated following challenge of shrimp with Vibrio anguillarum and white spot syndrome virus (WSSV). MjLTL2 can agglutinate several bacteria without Ca 2+ . In addition, MjLTL2 could bind to several Gram-positive and -negative bacteria by binding to their lipopolysaccharide and peptidoglycan. However, MjLTL2 could not enhance the clearance of V. anguillarum in vivo. In the presence of WSSV infection, MjLTL2 knockdown by RNA interference resulted in a 7day lower cumulative mortality of M. japonicus. Moreover, less VP19, VP24, VP26, and VP28 mRNAs were extracted from the hemocytes of MjLTL2 knockdown shrimp than from the control. These results suggest that MjLTL2 is involved in immune responses in shrimp.

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Section: Discussionmentioning

confidence: 99%

Identification and characterization of a novel L-type lectin (MjLTL2) from kuruma shrimp (Marsupenaeus japonicus)

Jing

Liu

et al. 2020

Fish & Shellfish Immunology

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“…Drosophila is a genetically tractable model host that is phylogenetically related to shrimp (Pan et al, 2017). The transgenic Drosophila model has proven to be a favorable system for studying the function of various viral proteins on the wholeorganism level (Hughes et al, 2012).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…This behavior is a potential immune evasion strategy that blocks the transcription of antiviral genes that would interfere with viral replication. The WSSV immediate early protein WSV187 can induce the upregulation of STAT92E to promote antiviral defense (Pan et al, 2017). The modulation of the JAK/STAT pathway through positive and negative approaches may contribute to the maintenance of the dynamic balance between viral replication and host survival.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

WSV181 inhibits JAK/STAT signaling and promotes viral replication in Drosophila

Wang

Pan²,

Huang

et al. 2019

Developmental & Comparative Immunology

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The Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway plays a critical role in host defense against viral infections. Here, we report the use of the Drosophila model system to investigate the modulation of the JAK/STAT pathway by the white spot syndrome virus (WSSV) protein WSV181. WSV181 overexpression in transgenic flies resulted in the downregulation of STAT92E and STAT92E-targeted genes. This result indicates that WSV181 can suppress JAK/STAT signaling by controlling STAT92E expression. An infection experiment was carried out on transgenic Drosophila infected with Drosophila C virus and on Litopenaeus vannamei injected with recombinant WSV181 and WSSV. The increased viral load and suppressed transcript levels of JAK/STAT pathway components indicate that WSV181 can promote viral proliferation by inhibiting the JAK/STAT pathway. This study provided evidence for the role of WSV181 in viral replication and revealed a new mechanism through which WSSV evades host immunity to maintain persistent infection.

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“…In the previous study, transgenic fly lines, each expressing one WSSV protein, were constructed to characterize the function of WSSV proteins on the whole-organism level ( Pan et al, 2017 ; Wang et al, 2019 ). Microarray data analysis in transgenic flies with or without WSV056 gene expression revealed sepiapterin reductase (Spr) gene CG12116 was most significantly inhibited by WSV056.…”

Section: Introductionmentioning

confidence: 99%

WSV056 Inhibits Shrimp Nitric Oxide Synthase Activity by Downregulating Litopenaeus vannamei Sepiapterin Reductase to Promote White Spot Syndrome Virus Replication

et al. 2021

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Sepiapterin reductase (Spr) plays an essential role in the biosynthesis of tetrahydrobiopterin (BH4), a key cofactor of multiple enzymes involved in various physiological and immune processes. Suppression of Spr could result in BH4 deficiency-caused diseases in human and murine models. However, information on the biological function of Spr in invertebrates is limited. In this study, two Sprs (CG12116 and Sptr) from Drosophila melanogaster were found to be downregulated in transgenic flies overexpressing white spot syndrome virus (WSSV) immediate-early protein WSV056. CG12116 and Sptr exerted an inhibitory effect on the replication of the Drosophila C virus. A Litopenaeus vannamei Spr (LvSpr) exhibiting similarity of 64.1–67.5% and 57.3–62.2% to that of invertebrate and vertebrate Sprs, respectively, were cloned. L. vannamei challenged with WSSV revealed a significant decrease in LvSpr transcription and Spr activity in hemocytes. In addition, the BH4 co-factored nitric oxide synthase (Nos) activity in shrimp hemocytes was reduced in WSSV-infected and LvSpr knockdown shrimp, suggesting WSSV probably inhibits the LvNos activity through LvSpr downregulation to limit the production of nitric oxide (NO). Knockdown of LvSpr and LvNos caused the reduction in NO level in hemocytes and the increase of viral copy numbers in WSSV-infected shrimp. Supplementation of NO donor DETA/NO or double gene knockdown of WSV056 + LvSpr and WSV056 + LvNos recovered the NO production, whereas the WSSV copy numbers were decreased. Altogether, the findings demonstrated that LvSpr and LvNos could potentially inhibit WSSV. In turn, the virus has evolved to attenuate NO production via LvSpr suppression by WSV056, allowing evasion of host antiviral response to ensure efficient replication.

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The immediate early protein WSV187 can influence viral replication via regulation of JAK/STAT pathway in Drosophila

Cited by 7 publications

References 55 publications

Identification and characterization of a novel L-type lectin (MjLTL2) from kuruma shrimp (Marsupenaeus japonicus)

Identification and characterization of a novel L-type lectin (MjLTL2) from kuruma shrimp (Marsupenaeus japonicus)

WSV181 inhibits JAK/STAT signaling and promotes viral replication in Drosophila

WSV056 Inhibits Shrimp Nitric Oxide Synthase Activity by Downregulating Litopenaeus vannamei Sepiapterin Reductase to Promote White Spot Syndrome Virus Replication

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