Characterization of an oligomerization domain and RNA-binding properties on rotavirus nonstructural protein NS34

Mattion, Nora; Cohen, Jean; Aponte, Carlos; Estes, Mary K.

doi:10.1016/0042-6822(92)91193-x

Cited by 53 publications

(54 citation statements)

References 40 publications

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“…Importance of the 59 UTR on the activity of the 39 TE+ A: RNAs were made that contained the 59 UTR of gene 6 and b-globin mRNAs and that lacked the last 68 (g6-Fluc⌬68, glo/g6-Fluc⌬68) and 106 (g6-Fluc⌬106, glo/g6-Fluc⌬106) bases of the g6-Fluc RNA+ Additional chimeras were made by adding the last 21 bases of the gene 6 39 UTR to these RNAs+ The chimeric g6-Fluc (B) and glo/g6-Fluc (C) RNAs were cotransfected with nv-Rluc into rotavirus-infected cells and, at 9 h postinfection, the levels of firefly and Renilla luciferases per milligram of cell lysate were determined+ The expression of firefly luciferase was normalized to the expression of Renilla luciferase+ The range reflects the values obtained in duplicate assays+ B C 39 translation enhancer of nonpolyadenylated mRNARNA polymerase, VP1, does as well (Patton, 1996)+ Because rotavirus mRNAs serve dual functions in the infected cell, it may be reasonable to propose that whether the mRNA is replicated or translated is determined by competition between VP1 and NSP3 for the 39 end+ However, that may not be the case, as VP1 accumulates in cytoplasmic inclusions, termed viroplasms, that form in infected cells and that are the sites of RNA replication and capsid assembly, whereas NSP3 accumulates on the cytoskeleton (Mattion et al+, 1992), the presumed site of mRNA translation+ If replication and translation occur in different places in the cell, then in fact VP1 and NSP3 may never compete for the same molecule of mRNA+…”

Section: Discussionmentioning

confidence: 99%

A four-nucleotide translation enhancer in the 3′-terminal consensus sequence of the nonpolyadenylated mRNAs of rotavirus

Chizhikov

Patton²

2000

RNA

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Section: Discussionmentioning

confidence: 99%

A four-nucleotide translation enhancer in the 3′-terminal consensus sequence of the nonpolyadenylated mRNAs of rotavirus

Chizhikov

Patton²

2000

RNA

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“…Three domains of activities have been mapped (31,32): the N-terminal part of the protein (aa 4 to 150) which binds specifically to the 3Ј end of the viral mRNAs; the middle For example, the fact that as opposed to NSP3, NSP3m was detected in Western blots depending on the presence of SDS in the lysis buffer might indicate a stronger interaction of NSP3m with some cellular components. This deserves further investigations, since the association of NSP3 with the cytoskeleton has been previously suggested (26). Gene rearrangements are thought to participate in the genetic variability of rotaviruses (9).…”

Section: Discussionmentioning

confidence: 99%

A Human Rotavirus with Rearranged Genes 7 and 11 Encodes a Modified NSP3 Protein and Suggests an Additional Mechanism for Gene Rearrangement

Gault

Schnepf

Poncet

et al. 2001

J Virol

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A human rotavirus (isolate M) with an atypical electropherotype with 14 apparent bands of double-stranded RNA was isolated from a chronically infected immunodeficient child. MA-104 cell culture adaptation showed that the M isolate was a mixture of viruses containing standard genes (M0) or rearranged genes: M1 (containing a rearranged gene 7) and M2 (containing rearranged genes 7 and 11). The rearranged gene 7 of virus M1 (gene 7R) was very unusual because it contained two complete open reading frames (ORF). Moreover, serial propagation of virus M1 in cell culture indicated that gene 7R rapidly evolved, leading to a virus with a deleted gene 7R (gene 7R⌬). Gene 7R⌬ coded for a modified NSP3 protein (NSP3m) of 599 amino acids (aa) containing a repetition of aa 8 to 296. The virus M3 (containing gene 7R⌬) was not defective in cell culture and actually produced NSP3m. The rearranged gene 11 (gene 11R) had a more usual pattern, with a partial duplication leading to a normal ORF followed by a long 3 untranslated region. The rearrangement in gene 11R was almost identical to some of those previously described, suggesting that there is a hot spot for gene rearrangements at a specific location on the sequence. It has been suggested that in some cases the existence of short direct repeats could favor the occurrence of rearrangement at a specific site. The computer modeling of gene 7 and 11 mRNAs led us to propose a new mechanism for gene rearrangements in which secondary structures, besides short direct repeats, might facilitate and direct the transfer of the RNA polymerase from the 5 to the 3 end of the plus-strand RNA template during the replication step.

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“…Cytoskeleton alterations could be an important stage in rotavirus-induced intestinal epithelial cell injury. Several studies have described the interactions of rotavirus with the cytoskeleton in MA104 (13,24), CV-1 (40), or BHK21 (27) unpolarized cell lines. Cytoskeleton alteration was also observed in a rotavirus-infected neuronal cell line (41).…”

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confidence: 99%

Rotavirus Infection Induces Cytoskeleton Disorganization in Human Intestinal Epithelial Cells: Implication of an Increase in Intracellular Calcium Concentration

Brunet

Jourdan

Cotte‐Laffitte

et al. 2000

J Virol

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Rotavirus infection is the most common cause of severe infantile gastroenteritis worldwide. In vivo, rotavirus exhibits a marked tropism for the differentiated enterocytes of the intestinal epithelium. In vitro, differentiated and undifferentiated intestinal cells can be infected. We observed that rotavirus infection of the human intestinal epithelial Caco-2 cells induces cytoskeleton alterations as a function of cell differentiation. The vimentin network disorganization detected in undifferentiated Caco-2 cells was not found in fully differentiated cells. In contrast, differentiated Caco-2 cells presented Ca 2؉-dependent microtubule disassembly and Ca 2؉ -independent cytokeratin 18 rearrangement, which both require viral replication. We propose that these structural alterations could represent the first manifestations of rotavirus-infected enterocyte injury leading to functional perturbations and then to diarrhea.Rotaviruses, members of the Reoviridae family, are recognized as the most important cause of viral gastroenteritis in young children. Although much is known about their replication and maturation processes, the pathophysiologic mechanisms by which rotavirus infection induces diarrhea remain unclear. Cytoskeleton alterations could be an important stage in rotavirus-induced intestinal epithelial cell injury. Several studies have described the interactions of rotavirus with the cytoskeleton in MA104 (13, 24), CV-1 (40), or BHK21 (27) unpolarized cell lines. Cytoskeleton alteration was also observed in a rotavirus-infected neuronal cell line (41). Whereas the cells on the sides of microvilli, which do not totally display the morphologic and functional characteristics of mature enterocytes, can be infected by rotavirus, mature enterocytes on tips of the villi constitute the human rotavirus main target cells (8,9). In order to approach the in vivo situation and to gain further insights into the pathophysiologic mechanisms of rotavirus infection, we and others have used the human intestinal epithelial cell lines 15,17,35) and 21,30,33,34). Since rotavirus can infect both undifferentiated and differentiated Caco-2 cells (16,18,35), this cell line, which spontaneously differentiates in culture, represents, like HT-29 cells, an attractive model to study the mechanisms of pathogenicity of rotavirus as a function of cell differentiation. It was reported by Michelangeli et al. (25) that the OSU strain of porcine rotavirus leads to an elevation in intracellular calcium concentration ([Ca 2ϩ ] i ) in MA104 cells. Using differentiated Caco-2 cells, which display many of the morphological and functional properties of mature enterocytes (22, 31), we recently reported that the simian rhesus rotavirus strain RRV induces an increase in [Ca 2ϩ ] i which is responsible for microvillar F-actin disassembly (5). This alteration is concomitant with a decrease in the activity and apical expression of the brush border-associated hydrolase sucrase-isomaltase (SI), which results from a profound perturbation in the intracellular...

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Characterization of an oligomerization domain and RNA-binding properties on rotavirus nonstructural protein NS34

Cited by 53 publications

References 40 publications

A four-nucleotide translation enhancer in the 3′-terminal consensus sequence of the nonpolyadenylated mRNAs of rotavirus

A four-nucleotide translation enhancer in the 3′-terminal consensus sequence of the nonpolyadenylated mRNAs of rotavirus

A Human Rotavirus with Rearranged Genes 7 and 11 Encodes a Modified NSP3 Protein and Suggests an Additional Mechanism for Gene Rearrangement

Rotavirus Infection Induces Cytoskeleton Disorganization in Human Intestinal Epithelial Cells: Implication of an Increase in Intracellular Calcium Concentration

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