Foot‐and‐mouth disease virus nonstructural protein 2B interacts with cyclophilin A, modulating virus replication

Liu, Huisheng; Xue, Qiao; Cao, Weijun; Yang, Fan; Ma, Linna; Liu, Wenjie; Zhang, Keshan; Liu, Xiangtao; Zhu, Zixiang; Zheng, Haixue

doi:10.1096/fj.201701351

Cited by 23 publications

(27 citation statements)

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“…The proteins VP0, VP1, VP3, L pro , 2B, 3A, and 3C pro play roles in inhibiting the host innate immune response (Li et al , 2016aZhu et al 2016;Fan et al 2017;Rodriguez Pulido and Saiz 2017;Rodriguez Pulido and Sanchez-Aparicio 2018). Additionally, host cell proteins that interact with VP1, 2B, 2C, and 3A have been identified using the yeast two-hybrid system (Gladue et al 2012(Gladue et al , 2014Liu et al 2017Liu et al , 2018. 3D is an important viral protein that has multiple roles in FMDV replication and pathogenesis (Rai et al 2013;Herod et al 2016;Rai et al 2017).…”

Section: Introductionmentioning

confidence: 99%

The DEAD-Box RNA Helicase DDX1 Interacts with the Viral Protein 3D and Inhibits Foot-and-Mouth Disease Virus Replication

et al. 2019

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Foot-and-mouth disease virus (FMDV) can infect domestic and wild cloven-hoofed animals. The non-structural protein 3D plays an important role in FMDV replication and pathogenesis. However, the interaction partners of 3D, and the effects of those interactions on FMDV replication, remain incompletely elucidated. In the present study, using the yeast two-hybrid system, we identified a porcine cell protein, DEAD-box RNA helicase 1 (DDX1), which interacted with FMDV 3D. The DDX1-3D interaction was further confirmed by co-immunoprecipitation experiments and an indirect immunofluorescence assay (IFA) in porcine kidney 15 (PK-15) cells. DDX1 was reported to either inhibit or facilitate viral replication and regulate host innate immune responses. However, the roles of DDX1 during FMDV infection remain unclear. Our results revealed that DDX1 inhibited FMDV replication in an ATPase/helicase activity-dependent manner. In addition, DDX1 stimulated IFN-b activation in FMDV-infected cells. Together, our results expand the body of knowledge regarding the role of DDX1 in FMDV infection.Keywords Foot-and-mouth disease virus (FMDV) Á Interaction Á DEAD-box RNA helicase 1 (DDX1) Á Antiviral function Á Interferon Electronic supplementary material The online version of this article (https://doi.

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Section: Introductionmentioning

confidence: 99%

The DEAD-Box RNA Helicase DDX1 Interacts with the Viral Protein 3D and Inhibits Foot-and-Mouth Disease Virus Replication

et al. 2019

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“…Cyclophilins, also known as peptidyl-prolyl cis-trans-isomerases, are ubiquitous proteins involved in multiple biological processes, including protein folding and trafficking, cell signaling, and immune responses (41). They have also been shown to promote or prevent virus infection (42,43). For example, cyclophilin A was found to bind to viral RNA to inhibit the replication of tomato bushy stunt virus (genus Tombusvirus, family Tombusviridae) in plant leaf cells (44), while cyclophilins of the aphid vector Schizaphis graminum have been shown to play an important role in cereal yellow dwarf virus (genus Polerovirus, family Luteoviridae) transmission (45).…”

Section: Discussionmentioning

confidence: 99%

Discovery of Novel Thrips Vector Proteins That Bind to the Viral Attachment Protein of the Plant Bunyavirus Tomato Spotted Wilt Virus

Badillo-Vargas¹,

Chen

Martin

et al. 2019

J Virol

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The plant-pathogenic virus tomato spotted wilt virus (TSWV) encodes a structural glycoprotein (GN) that, like with other bunyavirus/vector interactions, serves a role in viral attachment and possibly in entry into arthropod vector host cells. It is well documented that Frankliniella occidentalis is one of nine competent thrips vectors of TSWV transmission to plant hosts. However, the insect molecules that interact with viral proteins, such as GN, during infection and dissemination in thrips vector tissues are unknown. The goals of this project were to identify TSWV-interacting proteins (TIPs) that interact directly with TSWV GN and to localize the expression of these proteins in relation to virus in thrips tissues of principal importance along the route of dissemination. We report here the identification of six TIPs from first-instar larvae (L1), the most acquisition-efficient developmental stage of the thrips vector. Sequence analyses of these TIPs revealed homology to proteins associated with the infection cycle of other vector-borne viruses. Immunolocalization of the TIPs in L1 revealed robust expression in the midgut and salivary glands of F. occidentalis, the tissues most important during virus infection, replication, and plant inoculation. The TIPs and GN interactions were validated using protein-protein interaction assays. Two of the thrips proteins, endocuticle structural glycoprotein and cyclophilin, were found to be consistent interactors with GN. These newly discovered thrips protein-GN interactions are important for a better understanding of the transmission mechanism of persistent propagative plant viruses by their vectors, as well as for developing new strategies of insect pest management and virus resistance in plants. IMPORTANCE Thrips-transmitted viruses cause devastating losses to numerous food crops worldwide. For negative-sense RNA viruses that infect plants, the arthropod serves as a host as well by supporting virus replication in specific tissues and organs of the vector. The goal of this work was to identify thrips proteins that bind directly to the viral attachment protein and thus may play a role in the infection cycle in the insect. Using the model plant bunyavirus tomato spotted wilt virus (TSWV), and the most efficient thrips vector, we identified and validated six TSWV-interacting proteins from Frankliniella occidentalis first-instar larvae. Two proteins, an endocuticle structural glycoprotein and cyclophilin, were able to interact directly with the TSWV attachment protein, GN, in insect cells. The TSWV GN-interacting proteins provide new targets for disrupting the viral disease cycle in the arthropod vector and could be putative determinants of vector competence.

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“…Cyclophilins, also known as peptidyl-prolyl cis-trans isomerases, are ubiquitous proteins involved in multiple biological processes, including protein folding and trafficking, cell signaling, and immune responses (39). They have also been shown to promote or prevent virus infection (40, 41), for example, cyclophilin A was found to bind to viral RNA to inhibit replication of Tomato bushy stunt virus (genus Tombusvirus , family Tombusviridae ) in plant leaf cells (42), while cyclophilins of the aphid vector Schizaphis graminum have been shown to play an important role in Cereal yellow dwarf virus (genus Polerovirus , family Luteoviridae ) transmission (43). Interactions between the thrips cyclophilin TIP (with G N ) documented in the present study may affect similar virus processes, such as virus replication and maturation, or thrips transmission and vector competence (43, 44).…”

Section: Discussionmentioning

confidence: 99%

Discovery of novel thrips vector proteins that bind to the viral attachment protein of the plant bunyavirus, tomato spotted wilt virus

Badillo-Vargas¹,

Chen

Martin

et al. 2018

Preprint

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16The plant-pathogenic virus, tomato spotted wilt virus (TSWV), encodes a structural 17 glycoprotein (G N ) that, like with other bunyavirus/vector interactions, serves a role in viral 18 attachment and possibly entry into arthropod vector host cells. It is well documented that 19Frankliniella occidentalis is one of seven competent thrips vectors of TSWV transmission to 20 plant hosts, however, the insect molecules that interact with viral proteins, such as G N , during 21 infection and dissemination in thrips vector tissues are unknown. The goals of this project 22 Importance Statement 37 Thrips-transmitted viruses cause devastating losses to numerous food crops worldwide. For 38 negative-sense RNA viruses that infect plants, the arthropod serves as a host as well by 39 supporting virus replication in specific tissues and organs of the vector. The goal of this work 40 was to identify vector/host proteins that bind directly to the viral attachment protein and thus 41 may play a role in the infection cycle in the insect. Using the model plant bunyavirus, tomato 42 spotted wilt virus (TSWV), and the most efficient thrips vector, we identified and validated 43 six TSWV-interacting proteins from Frankliniella occidentalis first instar larvae. Two 44 proteins, an endocuticle structural glycoprotein and cyclophilin, were able to interact directly 45 with the TSWV attachment protein, G N, in insect cells. The TSWV G N -interacting proteins 46 3 provide new targets for disrupting the virus-vector interaction and could be putative 47 determinants of vector competence. 48 49Vector-borne diseases caused by animal-and plant-infecting viruses are some of the 50 most important medical, veterinary, and agricultural problems worldwide (1, 2). The majority 51 of viruses infecting plants and animals are transmitted by arthropods. Understanding the viral 52 and arthropod determinants of vector competence is important for basic knowledge of virus-53 vector interactions and development of new interdiction strategies to control disease. 54Significant progress has been made towards identification of viral determinants of 55 transmission, but the interacting molecules in vectors remain largely elusive. For negative-56 sense RNA viruses, vector factors that mediate the transmission process have not been well 57 characterized. 58Bunyavirales is the largest order of negative-sense RNA viruses; twelve families are 59 described (http://www.ictvonline.org/virustaxonomy.asp). The Bunyavirales contains plant 60 and insect vector-infecting viruses that make up the Family Tospoviridae (3-5). Within this 61 family, there are eighteen species and several unassigned viruses that most likely will be 62 classified as unequivocal members of the Orthotospovirus genus. Tomato spotted wilt 63 orthotospovirus is the type species within this genus and has been best characterized in terms 64 of viral host range, genome organization and protein functions (6, 7). 65 Tomato spotted wilt virus (TSWV) infects both monocotyledonous and dicotyledonous 66 plants enc...

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Foot‐and‐mouth disease virus nonstructural protein 2B interacts with cyclophilin A, modulating virus replication

Cited by 23 publications

References 44 publications

The DEAD-Box RNA Helicase DDX1 Interacts with the Viral Protein 3D and Inhibits Foot-and-Mouth Disease Virus Replication

The DEAD-Box RNA Helicase DDX1 Interacts with the Viral Protein 3D and Inhibits Foot-and-Mouth Disease Virus Replication

Discovery of Novel Thrips Vector Proteins That Bind to the Viral Attachment Protein of the Plant Bunyavirus Tomato Spotted Wilt Virus

Discovery of novel thrips vector proteins that bind to the viral attachment protein of the plant bunyavirus, tomato spotted wilt virus

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