Electron microscopy of Nicotiana glutinosa leaf cells infected with potato virus X

Stols, A.L.H.; Meulen, G.W. Hill-van der; Toen, M.K.I.

doi:10.1016/0042-6822(70)90389-2

Cited by 20 publications

(14 citation statements)

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“…The clearly evident substructure noted on DVX particles negatively stained with uranyl formate is also a feature reported for other potexviruses (Varma et al 1968). The aggregates of DVX-like particles closely packed in parallel in DVX-infected peas resemble those reported for clover yellow mosaic virus (CYMV) by Purcifull et al (1966) and for potato virus X (PVX) by Stols et at. (1970).…”

Section: Discussionsupporting

confidence: 59%

Daphne virus X: A potexvirus from daphne

Forster

Milne

1978

New Zealand Journal of Agricultural Research

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Daphne virus X (DVX) was found in all specimens of Daphne cneorum L. indexed for virus but was not associated with macroscopic symptoms. Experimental hosts of DVX included 18 species from 6 dicotyledonous families. Inl'ectivity was retained in expressed sap of Nicotiana clevelandii Gray for 5 weeks at c. 20°c. in sap diluted to 10-5 , after heating for 10 min at 80°c. Attempts to transmit DVX with Myzus persicae (Sulz) failed. DVX was purified lrom N. clevelandii leaves using chloroform: n-butanol clarification, one cycle of differential. then density-gradient, centrifugation. Preparations had a 260: 280 ratio of 1.22, a sedimentation coefficient of 110 S, and a buoyant density in CsCl of 1.28 g/m!. An antiserum to DVX had a titre of 1: 2048. DVX was not serologically related to clover yellow mosaic virus, narcissus mosaic virus, potato virus X, and white clover mosaic virus. The flexuous filamentous particles of DVX had a normal length of 499 nm in negatively stained preparations from LJ. cneorum flowers. Ultra-thin sections of pea leaflets systematically infected with DVX contained aggregates of DVX-like particles as well as unaggregated particles scattered in the cytoplasm. It is proposed that DVX is ::i distinct potexvirus. The present cryptogram for DVX is

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Section: Discussionsupporting

confidence: 59%

Daphne virus X: A potexvirus from daphne

Forster

Milne

1978

New Zealand Journal of Agricultural Research

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“…1, A and B;Kozar and Sheludko, 1969;Stols et al, 1970;Shalla and Shepard, 1972). Recently, we found that a C-terminal TGB1-mCherry fusion, expressed ectopically from a 35S promoter within infected tissue, is localized in aggregates inside the X-body, morphologically similar to the beaded sheets (Tilsner et al, 2009).…”

Section: Tgb1mentioning

confidence: 99%

“…In infected tissue, N-terminal GFP-TGB1 has been observed in plasmodesmata and aggregates (Samuels et al, 2007). In electron microscopy (EM), large proteinaceous aggregates in the form of "beaded sheets" are typical for PVX infections (Kozar and Sheludko, 1969;Stols et al, 1970;Shalla and Shepard, 1972), and these are heavily decorated with antibodies against TGB1 (Davies et al, 1993;Santa Cruz et al, 1998). The protein also has a strong tendency to oligomerize in vitro (Leshchiner et al, 2008), indicating that the aggregates observed with FP fusions to TGB1 may not be fusion-dependent artifacts.…”

mentioning

confidence: 99%

“…In mature PVX infections, the bulk of the vRNA was localized in circular "whorls" within the perinuclear X-body. The X-body also harbors the beaded sheets that contain TGB1 (Kozar and Sheludko, 1969;Stols et al, 1970;Shalla and Shepard, 1972;Davies et al, 1993;Santa Cruz et al, 1998). A fluorescent TGB1-mCherry fusion was localized precisely to the center of the RNA whorls (Tilsner et al, 2009), prompting us to investigate the role of TGB1 in the organization of the PVX X-body in more detail.…”

mentioning

confidence: 99%

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The TGB1 Movement Protein ofPotato virus XReorganizes Actin and Endomembranes into the X-Body, a Viral Replication Factory

et al. 2012

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Potato virus X (PVX) requires three virally encoded proteins, the triple gene block (TGB), for movement between cells. TGB1 is a multifunctional protein that suppresses host gene silencing and moves from cell to cell through plasmodesmata, while TGB2 and TGB3 are membrane-spanning proteins associated with endoplasmic reticulum-derived granular vesicles. Here, we show that TGB1 organizes the PVX “X-body,” a virally induced inclusion structure, by remodeling host actin and endomembranes (endoplasmic reticulum and Golgi). Within the X-body, TGB1 forms helically arranged aggregates surrounded by a reservoir of the recruited host endomembranes. The TGB2/3 proteins reside in granular vesicles within this reservoir, in the same region as nonencapsidated viral RNA, while encapsidated virions accumulate at the outer (cytoplasmic) face of the X-body, which comprises a highly organized virus “factory.” TGB1 is both necessary and sufficient to remodel host actin and endomembranes and to recruit TGB2/3 to the X-body, thus emerging as the central orchestrator of the X-body. Our results indicate that the actin/endomembrane-reorganizing properties of TGB1 function to compartmentalize the viral gene products of PVX infection.

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“…Small squares (1 mm 2) of leaf tissue of plants heavily inoculated with purified virus were taken daily during a period of ten days after inoculation. The samples were fixed, washed, cut and stained as described by Stols et al (1970). Thin sections were viewed in a Philips EM 200.…”

mentioning

confidence: 99%