Electron microscopic study of the formation of poliovirus

Dales, Samuel; Eggers, Hans J.; Tamm, Igor; Palade, George E.

doi:10.1016/0042-6822(65)90001-2

Cited by 305 publications

(242 citation statements)

References 16 publications

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“…Similar observation was reported for enteroviruses [3]. These large polyribosomes presumably are synthesizing virus-directed proteins.…”

Section: Electron Microscopysupporting

confidence: 64%

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1971

Japanese Journal of Microbiology

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Human embryo lung cells infected with rhinovirus type 2 (HGP strain) were sampled at intervals during viral growth and thin sections examined by electron microscopy. Infectivity assay showed an increase of intracellular virus 7 to 8 hr postinoculation and a peak titer at 16 to 18 hr. Changes resulting from infection, as revealed by electron microscopy, comprised (i) the appearance in the cytoplasm, at 8 hr postinfection, of large ribosomal clusters, membrane-enclosed bodies which proliferated extensively in the central zone of the cell, and viroplasm, aggregates of irregularly dense, coarse, granular material, and (ii) the appearance in the cytoplasm, at 16 hr postinoculation, of recognizable progeny virus particles. The particles were aligned along parallel fibrils or were found singly in some instances. As incubation continued, the particles became increasingly more spherical, and formed parallel long rows, and (iii) eventually, 24 hr after inoculation, formed closely packed viral crystals of a rectangular or hexagonal lattice. The mature progeny particles were 26 to 28 m diameter. These changes were reminiscent of those reported previously for the polio and other enteroviruses.The present knowledge of replication of rhinoviruses as revealed by electron microscopy is very limited. Hamparian et al. [6] observed spherical structures in crystalline arrays in the cytoplasm of human diploid fetal lung cultures infected with a rhinovirus. Blough et al. [1] investigated the effect of magnesium on the formation of intracellular virus crystals in HeLa cells infected with type 2 rhinovirus and proposed the close-packed cubic arrangement as the most probable configuration of the crystal.This report deals with the electron microscopic observation of human fetal lung strain cells infected with strain HGP of rhinovirus type 2. The essential features of the changes observed in infected cells were quite reminiscent of those described previously for polio and other enteroviruses. MATERIALS AND METHODSCell cultures. Cell strains, ML-9 and NL-17, of human embryo lung (HEL) were used at the 10th to 20th subculture. The culture technique was described earlier [9]. Eagle's minimum essential medium containing 20% calf serum was used for cell growth. After virus inoculation the concentration of calf serum in the medium was reduced to 2%.

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“…Similar observation was reported for enteroviruses [3]. These large polyribosomes presumably are synthesizing virus-directed proteins.…”

Section: Electron Microscopysupporting

confidence: 64%

“…The latter structure (Fig. 4) is undoubtedly homologous with the viroplasm described for polioviruses and other enteroviruses [3]. Large aggregates of ribosomes, presumably polyribosomes, were observed in the cytoplasmic matrix.…”

Section: Electron Microscopymentioning

confidence: 72%

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1971

Japanese Journal of Microbiology

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“…2E) in the host cell's cytoplasmic area. Both crystalline array formation and unordered aggregation within the cytoplasm are common features of several ssRNA viruses infectious to plants (36,56), picornaviruses infectious to animals (11,24), and marine algal ssRNA viruses (HaRNAV and HcRNAV) (61,63). It was also notable that the virus particles were concentrated along the intracellular membrane structures (Fig.…”

Section: Resultsmentioning

confidence: 93%

Isolation and Characterization of a Novel Single-Stranded RNA Virus Infectious to a Marine Fungoid Protist, Schizochytrium sp. (Thraustochytriaceae, Labyrinthulea)

Takao

Nagasaki

Mise

et al. 2005

Appl Environ Microbiol

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Thraustochytrids are cosmopolitan osmoheterotrophic microorganisms that play important roles as decomposers, producers of polyunsaturated fatty acids, and pathogens of mollusks, especially in coastal ecosystems. SssRNAV, a novel single-stranded RNA (ssRNA) virus infecting the marine fungoid protist Schizochytrium sp. (Labyrinthulea, Thraustochytriaceae) was isolated from the coastal water of Kobe Harbor, Japan, in July 2000, and its basic characteristics were examined. The virus particle is icosahedral, lacks a tail, and is ca. 25 nm in diameter. SssRNAV formed crystalline arrays and random assemblies within the cytoplasm of host cells, and it was also concentrated along the intracellular membrane structures. By means of one-step growth experiments, the lytic cycle and the burst size were estimated to be <8 h and 5.8 ؋ 10 3 to 6.4 ؋ 10 4 infectious units per host cell, respectively. SssRNAV had a single molecule of ssRNA that was approximately 10.2 kb long, three major proteins (37, 34, and 32 kDa), and two minor proteins (80 and 18 kDa). Although SssRNAV was considered to have some similarities with invertebrate viruses belonging to the family Dicistroviridae based on its partial nucleotide sequence, further genomic analysis is required to determine the detailed classification and nomenclature of SssRNAV. Our results indicate that viral infection is one of the significant factors controlling the dynamics of thraustochytrids and provide new insights into understanding the ecology of these organisms.

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“…These structures are derived sequentially from membranes of different cellular organelles. At early times following infection, PV-induced vesicles are probably formed in the ER (3,5,37), whereas at later times, membranes from other cellular organelles, including lysosomes and the Golgi apparatus, may also contribute to vesicle formation (4,5). RTN3 is an ER-associated protein, and its reduced expression in knockdown cells may affect the budding of replication complex vesicles manufactured from the ER compartment membrane (Fig.…”

Section: Discussionmentioning

confidence: 99%

Reticulon 3 Binds the 2C Protein of Enterovirus 71 and Is Required for Viral Replication

Tang¹,

Yang²,

Wu³

et al. 2007

Journal of Biological Chemistry

141

124

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Enterovirus 71 is an enterovirus of the family Picornaviridae. The 2C protein of poliovirus, a relative of enterovirus 71, is essential for viral replication. The poliovirus 2C protein is associated with host membrane vesicles, which form viral replication complexes where viral RNA synthesis takes place. We have now identified a host-encoded 2C binding protein called reticulon 3, which we found to be associated with the replication complex through direct interaction with the enterovirus 71-encoded 2C protein. We observed that the N terminus of the 2C protein, which has both RNA-and membrane-binding activity, interacted with reticulon 3. This region of interaction was mapped to its reticulon homology domain, whereas that of 2C was encoded by the 25th amino acid, isoleucine. Reticulon 3 could also interact with the 2C proteins encoded by other enteroviruses, such as poliovirus and coxsackievirus A16, implying that it is a common factor for such viral replication. Reduced production of reticulon 3 by RNA interference markedly reduced the synthesis of enterovirus 71-encoded viral proteins and replicative doublestranded RNA, reducing plaque formation and apoptosis. Furthermore, reintroduction of nondegradable reticulon 3 into these knockdown cells rescued enterovirus 71 infectivity, and viral protein and double-stranded RNA synthesis. Thus, reticulon 3 is an important component of enterovirus 71 replication, through its potential role in modulation of the sequential interactions between enterovirus 71 viral RNA and the replication complex.

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Electron microscopic study of the formation of poliovirus

Cited by 305 publications

References 16 publications

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Isolation and Characterization of a Novel Single-Stranded RNA Virus Infectious to a Marine Fungoid Protist, Schizochytrium sp. (Thraustochytriaceae, Labyrinthulea)

Reticulon 3 Binds the 2C Protein of Enterovirus 71 and Is Required for Viral Replication

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