Host Factors in the Infection Cycle of Bamboo mosaic virus

Huang, Y. S.; Chen, I‐Hsuan; Tsai, Ching‐Hsiu

doi:10.3389/fmicb.2017.00437

Cited by 28 publications

(27 citation statements)

References 89 publications

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“…The study of differentially expressed genes after virus infection is a strategy for identifying host factors involved in virus infection cycles. We used a cDNA-AFLP technique to identify a number of these genes (Cheng et al ., 2010) and revealed their involvement in BaMV infection (Huang et al ., 2017a). One of the host factors in this study was demonstrated to play a defensive role against BaMV replication.…”

Section: Discussionmentioning

confidence: 99%

An E3 ubiquitin ligase fromNicotiana benthamianatargets the replicase ofBamboo mosaic virusand restricts its replication

Chen

Chang

et al. 2018

Preprint

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One up-regulated host gene identified previously was found involved in the infection process of Bamboo mosaic virus (BaMV), a single-stranded positive-sense RNA virus. The full length cDNA of this gene was cloned by 5′ and 3′-rapid amplification of cDNA ends and found to encode a polypeptide containing a conserved really interesting new gene (RING) domain and a transmembrane domain. The gene might function as an ubiquitin E3 ligase. We designated this protein in Nicotiana benthamiana as ubiquitin E3 ligase containing RING domain 1 (NbUbE3R1). Further characterization by using Tobacco rattle virus -based virus-induced gene silencing (loss-of-function) revealed that increased BaMV accumulation was in both knockdown plants and protoplasts. The gene might have a defensive role in the replication step of BaMV infection. To further inspect the functional role of NbUbE3R1 in BaMV accumulation, NbUbE3R1 was expressed in N. benthamiana plants. The wild-type NbUbE3R1-orange fluorescent protein (NbUbE3R1-OFP), NbUbE3R1/△TM-OFP (removal of the transmembrane domain) and NbUbE3R1/mRING-OFP (mutation at the RING domain, the E2 interaction site) were transiently expressed in plants. NbUbE3R1 and its derivatives all functioned in restricting the accumulation of BaMV. The common feature of these constructs was the intact substrate-interacting domain. Yeast two-hybrid and co-immunoprecipitation experiments used to determine the possible viral-encoded substrate of NbUbE3R1 revealed the replicase of BaMV as the possible substrate. In conclusion, we identified an up-regulated gene, NbUbE3R1 that plays a role in BaMV replication.

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Section: Discussionmentioning

confidence: 99%

An E3 ubiquitin ligase fromNicotiana benthamianatargets the replicase ofBamboo mosaic virusand restricts its replication

Chen

Chang

et al. 2018

Preprint

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“…As a native pathway of NbEILP for sensing the elicitors from pathogens, NbEILP is synthesized and retained on the ER membrane and is possibly secreted to the plasma membrane as vesicle trafficking. The movement complex containing TGBp1, vRNA, replicase, CP, TGBp2, and TGBp3 of BaMV ( Chou et al, 2013 ; Huang et al, 2017 ) might take advantage of the secretory path of NbEILP to reach the plasmodesmata for cell-to-cell movement. Therefore, the possible role of NbEILP in BaMV movement could be gathering these viral- or host-encoded movement-associated proteins together.…”

Section: Discussionmentioning

confidence: 99%

“…The coding capacity of a small viral RNA genome is limited to facilitate the infection and replication cycle; the RNA virus requires different host proteins directly or indirectly to assist its accumulation ( Ahlquist et al, 2003 ; Hyodo and Okuno, 2016 ; Nagy, 2016 ). A few host proteins associated with viral RNA or the RdRp complex are involved in BaMV replication such as the chloroplast phosphoglycerate kinase, heat-shock protein 90, and glutathione S -transferase U4 ( Huang et al, 2017 ). The host proteins RabGTPase-activating protein 1, serine/threonine kinase-like protein, and casein kinase 2α participate in BaMV movement ( Huang et al, 2017 ).…”

Section: Introductionmentioning

confidence: 99%

“…A few host proteins associated with viral RNA or the RdRp complex are involved in BaMV replication such as the chloroplast phosphoglycerate kinase, heat-shock protein 90, and glutathione S -transferase U4 ( Huang et al, 2017 ). The host proteins RabGTPase-activating protein 1, serine/threonine kinase-like protein, and casein kinase 2α participate in BaMV movement ( Huang et al, 2017 ).…”

Section: Introductionmentioning

confidence: 99%

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Nicotiana benthamiana Elicitor-Inducible Leucine-Rich Repeat Receptor-Like Protein Assists Bamboo Mosaic Virus Cell-to-Cell Movement

et al. 2017

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For successful infection, a virus requires various host factors at different stages such as translation, targeting, replication, and spreading. One of the host genes upregulated after Nicotiana benthamiana infection with Bamboo mosaic virus (BaMV), a single-stranded positive-sense RNA potexvirus, assists in viral movement. To understand how this host protein is involved in BaMV movement, we cloned its full-length cDNA by rapid amplification of cDNA ends. The gene has 3199 nt and encodes a 969-amino acid polypeptide. The sequence of the encoded polypeptide is orthologous to that of N. tabacum elicitor-inducible leucine-rich repeat (LRR) receptor-like protein (NtEILP), a plant viral resistance gene, and is designated NbEILP. To reveal how NbEILP is involved in BaMV movement, we fused green fluorescent protein (GFP) to its C-terminus. Unfortunately, the gene’s expression in N. benthamiana was beyond our detection limit possibly because of its large size (∼135 kDa). However, NbEILP at such low expression could still enhance BaMV accumulation in inoculated leaves. A short version of NbEILP was constructed to remove the LRR domain, NbEILP/ΔLRR-GFP; the expression of this deletion mutant could still enhance BaMV accumulation to 1.7-fold that of the control. Hence, the LRR domain in NbEILP is not an essential element in BaMV movement. We constructed a few deletion mutants — NbEILP/ΔLRRΔTMD (without the transmembrane domain), NbEILP/ΔLRRΔCD (without the cytoplasmic domain), and NbEILP/ΔLRRΔSP (without the signal peptide) — to examine whether these domains are involved in BaMV movement. For BaMV movement, NbEILP requires the signal peptide to target the endoplasmic reticulum and the transmembrane domain to retain on the membrane.

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“…Bamboo mosaic virus (BaMV) is a well-studied species in the genus Potexvirus, family Alphaflexiviridae Cheng, 2017;Huang et al, 2017). Its positive-strand RNA genome is 6366 nt (excluding the 3 0 poly(A) tail) and contains five open reading frames (Lin et al, 1994;Yang et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Nicotiana benthamiana Argonaute10 plays a pro‐viral role in Bamboo mosaic virus infection

Huang

Tsai

et al. 2019

New Phytologist

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Summary RNA silencing is a major defense mechanism against invading viruses in plants. Argonaute proteins (AGOs) are the key players in RNA silencing. The number of AGO family members involved varies depending on the plant species and they play distinct or sometimes redundant roles in antiviral defense. By using a virus‐induced gene silencing technique, it was found that Nicotiana benthamiana AGO1 restricted Bamboo mosaic virus (BaMV) accumulation, but NbAGO10, the closest paralog of NbAGO1, positively regulated BaMV accumulation. Immunoprecipitation assay revealed BaMV virus‐derived small interfering RNAs (vsiRNAs) in NbAGO10 complexes. Transient overexpression of NbAGO10 increased BaMV RNA accumulation, but with co‐expression of NbAGO1, BaMV RNA accumulation was reduced, which suggests that NbAGO10 may have competed with NbAGO1 for sequestering BaMV vsiRNA and prevented the formation of RNA‐induced silencing complexes. In addition, overexpression of NbAGO10 decreased BaMV vsiRNA accumulation. A host enzyme, small RNA degrading nuclease 1 (SDN1), also was found to interact with NbAGO10 on in vivo pull‐down assay. Silencing of SDN1 elevated BaMV vsiRNA level and decreased BaMV RNA accumulation in N. benthamiana, indicating that NbAGO10 might recruit SDN1 for BaMV vsiRNA degradation. The results herein suggested that NbAGO10 plays a pro‐viral role by BaMV vsiRNA sequestration and degradation.

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Host Factors in the Infection Cycle of Bamboo mosaic virus

Cited by 28 publications

References 89 publications

An E3 ubiquitin ligase fromNicotiana benthamianatargets the replicase ofBamboo mosaic virusand restricts its replication

An E3 ubiquitin ligase fromNicotiana benthamianatargets the replicase ofBamboo mosaic virusand restricts its replication

Nicotiana benthamiana Elicitor-Inducible Leucine-Rich Repeat Receptor-Like Protein Assists Bamboo Mosaic Virus Cell-to-Cell Movement

Nicotiana benthamiana Argonaute10 plays a pro‐viral role in Bamboo mosaic virus infection

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