A transmembrane domain determines the localization of rice stripe virus pc4 to plasmodesmata and is essential for its function as a movement protein

Our previous research found that NSvc4, the movement protein of rice stripe virus (RSV), could localize to the actin filaments, endoplasmic reticulum, plasmodesmata, and chloroplast, but the roles of NSvc4 played in the chloroplast were opaque. Here, we confirm the accumulation of NSvc4 in the chloroplasts and the N-terminal 1–73 amino acids of NSvc4 are sufficient to localize to chloroplasts. We provide evidence to show that chloroplast-localized NSvc4 can impair the chloroplast-mediated immunity. Expressing NSvc4 in Nicotiana benthamiana leaves results in the decreased expression of defense-related genes NbPR1, NbPR2, and NbWRKY12 and the inhibition of chloroplast-derived ROS production. In addition, generation of an infectious clone of potato virus X (PVX) carrying NSvc4 facilitates PVX infection in N. benthamiana plants. Moreover, we identify two chloroplast-related host factors, named NbGAPDH-A and NbPsbQ1, both of which can interact with NSvc4. Knockdown of NbGAPDH-A or NbPsbQ1 can both promote RSV infection. Our results decipher a detailed function of NSvc4 in the chloroplast.

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First evidence showing that Pepper vein yellows virus P4 protein is a movement protein

10.21203/rs.2.18235/v3 ◽

2020 ◽

Author(s):

Sangsang Li ◽

Xianyang Su ◽

Xiangwen Luo ◽

Yu Zhang ◽

Deyong Zhang ◽

...

Keyword(s):

Transmembrane Domain ◽

Movement Protein ◽

Protein S ◽

Bioinformatic Analysis ◽

Plant Viruses ◽

Specific Protein ◽

Virus Movement ◽

Genomic Rnas ◽

Pepper Vein Yellows Virus ◽

Substitution Mutant

Abstract Background Plant viruses move through plasmodesmata (PD) to infect new cells. To overcome the PD barrier, plant viruses have developed specific protein(s) to guide their genomic RNAs or DNAs to path through the PD. Results In the present study, we analyzed the function of Pepper vein yellows virus P4 protein. Our bioinformatic analysis showed that the P4 protein contains an transmembrane domain, encompassing the amino acid residue 117-138. The P4 protein was found to target PD and form small punctates near walls. The P4 deletion mutant or the substitution mutant lost their function to produce punctates near the walls inside the fluorescent loci. The P4-YFP fusion was found to move from cell to cell in infiltrated leaves, and P4 could complement Cucumber mosaic virus movement protein deficiency mutant to move between cells. Conclustion Taking together, we consider that the P4 protein is a movement protein of Pepper vein yellows virus.

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Pc4, a putative movement protein of Rice stripe virus, interacts with a type I DnaJ protein and a small Hsp of rice

Virus Genes ◽

10.1007/s11262-008-0324-z ◽

2009 ◽

Vol 38 (2) ◽

pp. 320-327 ◽

Cited By ~ 29

Author(s):

Lianming Lu ◽

Zhenguo Du ◽

Meiling Qin ◽

Ping Wang ◽

Hanhong Lan ◽

...

Keyword(s):

Movement Protein ◽

Rice Stripe Virus ◽

Type I ◽

Dnaj Protein ◽

Small Hsp ◽

Putative Movement Protein

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First evidence showing that Pepper vein yellows virus P4 protein is a movement protein

10.21203/rs.2.18235/v2 ◽

2020 ◽

Author(s):

Sangsang Li ◽

Xianyang Su ◽

Xiangwen Luo ◽

Yu Zhang ◽

Deyong Zhang ◽

...

Keyword(s):

Transmembrane Domain ◽

Movement Protein ◽

Protein S ◽

Bioinformatic Analysis ◽

Plant Viruses ◽

Specific Protein ◽

Virus Movement ◽

Genomic Rnas ◽

Pepper Vein Yellows Virus ◽

Substitution Mutant

Abstract Background Plant viruses move through plasmodesmata (PD) to infect new cells. To overcome the PD barrier, plant viruses have developed specific protein(s) to guide their genomic RNAs or DNAs to path through the PD. Results In the present study, we analyzed the function of Pepper vein yellows virus P4 protein. Our bioinformatic analysis showed that the P4 protein contains an transmembrane domain, encompassing the amino acid residue 117-138. The P4 protein was found to target PD and form small punctates near walls. The P4 deletion mutant or the substitution mutant lost their function to produce punctates near the walls inside the fluorescent loci. The P4-YFP fusion was found to move from cell to cell in infiltrated leaves, and P4 could complement Cucumber mosaic virus movement protein deficiency mutant to move between cells. Conclustion Taking together, we consider that the P4 protein is a movement protein of Pepper vein yellows virus.

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Plasmodesmal targeting and intercellular movement of potato mop-top pomovirus is mediated by a membrane anchored tyrosine-based motif on the lumenal side of the endoplasmic reticulum and the C-terminal transmembrane domain in the TGB3 movement protein

Virology ◽

10.1016/j.virol.2010.03.008 ◽

2010 ◽

Vol 402 (1) ◽

pp. 41-51 ◽

Cited By ~ 23

Author(s):

J. Tilsner ◽

G.H. Cowan ◽

A.G. Roberts ◽

S.N. Chapman ◽

A. Ziegler ◽

...

Keyword(s):

Endoplasmic Reticulum ◽

Transmembrane Domain ◽

Movement Protein ◽

Intercellular Movement

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First evidence showing that Pepper vein yellows virus P4 protein is a movement protein

10.21203/rs.2.18235/v1 ◽

2019 ◽

Author(s):

Sangsang Li ◽

Xianyang Su ◽

Xiangwen Luo ◽

Yu Zhang ◽

Deyong Zhang ◽

...

Keyword(s):

Transmembrane Domain ◽

Movement Protein ◽

Protein S ◽

Bioinformatic Analysis ◽

Plant Viruses ◽

Specific Protein ◽

Virus Movement ◽

Genomic Rnas ◽

Pepper Vein Yellows Virus ◽

Substitution Mutant

Abstract Background Plant viruses move through plasmodesmata (PD) to infect new cells. To overcome the PD barrier, plant viruses have developed specific protein(s) to guide their genomic RNAs or DNAs to path through the PD.Results In the present study, we analyzed the function of Pepper vein yellows virus P4 protein. Our bioinformatic analysis showed that the P4 protein contains an transmembrane domain, encompassing the amino acid residue 117-138. The P4 protein was found to target PD and form small punctates near walls. The P4 deletion mutant or the substitution mutant lost their function to produce punctates near the walls inside the fluorescent loci. The P4-YFP fusion was found to move from cell to cell in infiltrated leaves, and P4 could complement Cucumber mosaic virus movement protein deficiency mutant to move between cells.Conclusion Taking together, we consider that the P4 protein is a movement protein of Pepper vein yellows virus.

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The unfolded protein response plays dual roles in rice stripe virus infection through fine-tuning the movement protein accumulation

PLoS Pathogens ◽

10.1371/journal.ppat.1009370 ◽

2021 ◽

Vol 17 (3) ◽

pp. e1009370

Author(s):

Chenyang Li ◽

Yi Xu ◽

Shuai Fu ◽

Yu Liu ◽

Zongdi Li ◽

...

Keyword(s):

Virus Infection ◽

Movement Protein ◽

Rice Stripe Virus ◽

Fine Tuning ◽

Dual Roles ◽

Unfolded Protein ◽

Rsv Infection ◽

Autophagic Degradation ◽

The Unfolded Protein Response ◽

Protein Response

The movement of plant viruses is a complex process that requires support by the virus-encoded movement protein and multiple host factors. The unfolded protein response (UPR) plays important roles in plant virus infection, while how UPR regulates viral infection remains to be elucidated. Here, we show that rice stripe virus (RSV) elicits the UPR in Nicotiana benthamiana. The RSV-induced UPR activates the host autophagy pathway by which the RSV-encoded movement protein, NSvc4, is targeted for autophagic degradation. As a counteract, we revealed that NSvc4 hijacks UPR-activated type-I J-domain proteins, NbMIP1s, to protect itself from autophagic degradation. Unexpectedly, we found NbMIP1 stabilizes NSvc4 in a non-canonical HSP70-independent manner. Silencing NbMIP1 family genes in N. benthamiana, delays RSV infection, while over-expressing NbMIP1.4b promotes viral cell-to-cell movement. Moreover, OsDjA5, the homologue of NbMIP1 family in rice, behaves in a similar manner toward facilitating RSV infection. This study exemplifies an arms race between RSV and the host plant, and reveals the dual roles of the UPR in RSV infection though fine-tuning the accumulation of viral movement protein.

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Recombinant Human Soluble Thrombomodulin Delivers Bounded Thrombin to Antithrombin III: Thrombomodulin Associates with Free Thrombin and Is Recycled to Activate Protein C

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649597 ◽

1993 ◽

Vol 70 (03) ◽

pp. 418-422 ◽

Cited By ~ 23

Author(s):

Masaharu Aritomi ◽

Naoko Watanabe ◽

Rika Ohishi ◽

Komakazu Gomi ◽

Takao Kiyota ◽

...

Keyword(s):

Protein C ◽

Antithrombin Iii ◽

Transmembrane Domain ◽

Chinese Hamster Ovary Cells ◽

Time Lag ◽

Chinese Hamster ◽

Ovary Cells ◽

Soluble Thrombomodulin ◽

Simulation Based ◽

Recombinant Human Soluble Thrombomodulin

SummaryRecombinant human soluble thrombomodulin (rhs-TM), having no transmembrane domain or chondroitin sulfate, was expressed in Chinese hamster ovary cells. Interactions between rhs-TM, thrombin (Th), protein C (PC) and antithrombin III (ATIII) were studied. Equilibrium between rhs-TM and Th had no detectable time lag in clotting inhibition (K d = 26 nM) or PC activation (K d = 22 nM), while ATIII inhibited Th at a bimolecular rate constant = 5,200 M-1s-1 (K d <0.2 nM). A mixture of ATIII, Th and rhs-TM showed that ATIII reacted with Th slower than rhs-TM, whose presence did not affect the reaction between ATIII and Th. In a mixture of rhs-TM, ATIII and PC, the repeated addition of Th caused the repeated activation of PC; which was consistent with the Simulation based on the assumption that rhs-TM is recycled as a Th cofactor. From these results, we concluded that upon inhibition of the rhs-TM-Th complex by ATIII, rhs-TM is released to recombine with free Th and begins to activate PC, while the Th-ATIII complex does not affect rhs-TM-Th equilibrium.

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