Capsid Protein-Mediated Recruitment of Host DnaJ-Like Proteins Is Required for
            <i>Potato Virus Y</i>
            Infection in Tobacco Plants

Hofius, Daniel; Maier, Annette; Dietrich, Christof P.; Jungkunz, Isabel; Börnke, Frederik; Maiß, E.; Sonnewald, Uwe

doi:10.1128/jvi.01525-07

Cited by 117 publications

(87 citation statements)

References 73 publications

(100 reference statements)

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“…MPB2C and NtMPIP1 are involved in TMV cell-to-cell spread by interacting with TMV MP (Curin et al, 2007;Kragler et al, 2003). NtCPIP2a and NtCPIP2b act as potyviral susceptibility factors during Potato virus Y infection and along with heat shock protein 70, they act as plant chaperones and are essential for virus movement (Hofius et al, 2007). TOM1 and TOM3 proteins in Arabidopsis and N. tabacum are associated with the multiplication of TMV and tobamoviruses (Asano et al, 2005;Yamanaka et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Identification of Tobacco Proteins Associated with the Stem-Loop 1 RNAs of Potato virus X

Cho

Kim

2012

Molecules and Cells

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Section: Discussionmentioning

confidence: 99%

Identification of Tobacco Proteins Associated with the Stem-Loop 1 RNAs of Potato virus X

Cho

Kim

2012

Molecules and Cells

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“…Early in potyviral infection, excess CP is removed by means of HSP70/ CPIP-mediated proteasomal degradation (9), allowing viral RNA translation and replication to proceed efficiently in the absence of premature particle assembly. The J-domain protein CPIP, a cochaperone of HSP70, is essential for potyvirus infection (13) and has been shown to interact with CP, relieving the CP-mediated inhibition of viral RNA translation (9). A possible mechanism for this effect may involve competition between CP-CPIP and CP-CP interactions.…”

Section: Fig 6 Cpmentioning

confidence: 99%

“…In addition, a chaperone-mediated ubiquitin degradation pathway has been suggested to limit the amount of CP during the early stages of infection (9). The mechanism makes use of a J-domain HSP40 chaperone named CP interacting protein (CPIP) (13). A model was proposed in which CPIP delivers potyviral CP to the degradation pathway via HSP70 until the system is overpowered by a high level of CP accumulation, after which virion assembly may commence (9,14).…”

mentioning

confidence: 99%

Cotranslational Coat Protein-Mediated Inhibition of Potyviral RNA Translation

Besong-Ndika

Ivanov

Hafrén

et al. 2015

J Virol

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Potato virus A (PVA) is a single-stranded positive-sense RNA virus and a member of the family Potyviridae. The PVA coat protein (CP) has an intrinsic capacity to self-assemble into filamentous virus-like particles, but the mechanism responsible for the initiation of viral RNA encapsidation in vivo remains unclear. Apart from virion assembly, PVA CP is also involved in the inhibition of viral RNA translation. In this study, we show that CP inhibits PVA RNA translation in a dose-dependent manner, through a mechanism involving the CP-encoding region. Analysis of this region, however, failed to identify any RNA secondary structure(s) preferentially recognized by CP, suggesting that the inhibition depends on CP-CP rather than CP-RNA interactions. In agreement with this possibility, insertion of an in-frame stop codon upstream of the CP sequence led to a marked decrease in the inhibition of viral RNA translation. Based on these results, we propose a model in which the cotranslational interactions between excess CP accumulating in trans and CP translated from viral RNA in cis are required to initiate the translational repression. This model suggests a mechanism for how viral RNA can be sequestered from translation and specifically selected for encapsidation at the late stages of viral infection. IMPORTANCEThe main functions of the CP during potyvirus infection are to protect viral RNA from degradation and to transport it locally, systemically, and from host to host. Although virion assembly is a key step in the potyviral infectious cycle, little is known about how it is initiated and how viral RNA is selected for encapsidation. The results presented here suggest that CP-CP rather than CP-RNA interactions are predominantly involved in the sequestration of viral RNA away from translation. We propose that the cotranslational nature of these interactions may represent a mechanism for the selection of viral RNA for encapsidation. A better understanding of the mechanism of virion assembly may lead to development of crops resistant to potyviruses at the level of viral RNA encapsidation, thereby reducing the detrimental effects of potyvirus infections on food production. P lant viral coat proteins (CPs) are associated with surprisingly many functions during the infectious cycle. Besides their roles in encapsidation and movement, CPs are implicated in viral RNA translation and replication during the early stages of infection (see references 1, 2, and 3 for reviews). Some of these functions involve specific and nonspecific interactions with viral RNA (4-7). For several positive-sense RNA viruses, CP modulates translation and/or replication in a concentration-dependent manner (4, 5). In these viruses, higher CP concentrations repress RNA accumulation, whereas lower concentrations stimulate RNA accumulation and translation. Hence, depending on the amount of CP, the virus can regulate the progression of virus infection from genome replication and translation to virion assembly.The potyviral CP is produced together with repl...

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“…Viral coat protein (CP) is not required for localized cell-to-cell movement in TMV and also is not required for the systemic or localized movement of some other viruses such as Tobacco rattle virus, Tomato bushy stunt virus, or Barley stripe mosaic virus (9,30,36). However, CP is required for the movement of other viruses that move as nucleoprotein complexes through the PD, including the potexviruses (43), potyviruses (10), and several other viruses (4,35). The second model includes viruses that move through the PD in the forms of encapsidated particles.…”

Section: Rice Stripe Virus (Rsv) Is the Type Member Of The Genusmentioning

confidence: 99%

Identification of a Movement Protein of the Tenuivirus Rice Stripe Virus

Xiong

Zhou

et al. 2008

J Virol

139

133

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Rice stripe virus (RSV) is the type member of the genus Tenuivirus. RSV has four single-stranded RNAs and causes severe disease in rice fields in different parts of China. To date, no reports have described how RSV spreads within host plants or the viral and/or host factor(s) required for tenuivirus movement. We investigated functions of six RSV-encoded proteins using trans-complementation experiments and biolistic bombardment. We demonstrate that NSvc4, encoded by RSV RNA4, supports the intercellular trafficking of a movementdeficient Potato virus X in Nicotiana benthamiana leaves. We also determined that upon biolistic bombardment or agroinfiltration, NSvc4:enhanced green fluorescent protein (eGFP) fusion proteins localize predominantly near or within the walls of onion and tobacco epidermal cells. In addition, the NSvc4:eGFP fusion protein can move from initially bombarded cells to neighboring cells in Nicotiana benthamiana leaves. Immunocytochemistry using tissue sections from RSV-infected rice leaves and an RSV NSvc4-specific antibody showed that the NSvc4 protein accumulated in walls of RSV-infected leaf cells. Gel retardation assays revealed that the NSvc4 protein interacts with single-stranded RNA in vitro, a common feature of many reported plant viral movement proteins (MPs). RSV NSvc4 failed to interact with the RSV nucleocapsid protein using yeast two-hybrid assays. Taken together, our data indicate that RSV NSvc4 is likely an MP of the virus. This is the first report describing a tenuivirus MP. Rice stripe virus (RSV) is the type member of the genusTenuivirus (Association of Applied Biologists Descriptions of Plant Viruses website [http://www.dpvweb.net/dpv/showdpv .php?dpvnoϭ375]). RSV causes severe diseases in rice fields, especially in China, and is known to be transmitted by the small brown plant hopper (Laodelphax striatellus) in a persistent, circulative-propagative manner (8,46). RSV is an RNA virus with four segmented single-stranded genomes, contains seven open reading frames (ORFs), and uses a negative and ambisense coding strategy for replication and infection in plants ( Fig. 1) (32). RNA1 is negative sense and encodes a putative protein with a molecular mass of approximately 337 kDa; this protein is reported to be part of the RNA-dependent RNA polymerase and is associated with the RSV filamentous ribonucleoprotein (42). RNAs 2 to 4 are ambisense, and each RNA contains two ORFs, one in the 5Ј half of the viral RNA and the other in the 5Ј half of the viral cRNA. RNA2 encodes NS2 (about 22.8 kDa, with an unknown function) from the viral RNA and NSvc2 (94 kDa, a putative membrane glycoprotein) from the viral cRNA. RNA3 encodes a 23-kDa protein that functions as a suppressor of gene silencing (R. Xiong et al., unpublished data) and the nucleocapsid protein (NCP) (35 kDa). The nonstructural disease-specific protein (SP) (21.5 kDa) and NSvc4 (32.5 kDa, with unknown function) are encoded by RNA4 (14,15,31,38,47,48).Numerous studies have indicated that plant viruses encode specific proteins known...

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Capsid Protein-Mediated Recruitment of Host DnaJ-Like Proteins Is Required for Potato Virus Y Infection in Tobacco Plants

Cited by 117 publications

References 73 publications

Identification of Tobacco Proteins Associated with the Stem-Loop 1 RNAs of Potato virus X

Identification of Tobacco Proteins Associated with the Stem-Loop 1 RNAs of Potato virus X

Cotranslational Coat Protein-Mediated Inhibition of Potyviral RNA Translation

Identification of a Movement Protein of the Tenuivirus Rice Stripe Virus

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