Sequences of the four larger proteins of a porcine group C rotavirus and comparison with the equivalent group a rotavirus proteins

Brémont, Michel; Juste-lesage, P.; Chabanne-Vautherot, Danièle; Charpilienne, Annie; Cohen, Jean

doi:10.1016/0042-6822(92)90035-n

Cited by 36 publications

(26 citation statements)

References 37 publications

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“…We found that the VP1 proteins segregate phylogenetically according to the strain's group designation, as has been previously reported ( Fig. 2) (2,5,7,14,23,26,45). There is an abundance of A-VP1 sequence information, and several genotypes have been defined (11,23).…”

Section: Genetic Variation Among Group a B And C Rv Rdrpssupporting

confidence: 58%

“…There is an abundance of A-VP1 sequence information, and several genotypes have been defined (11,23). In contrast, only four B-VP1 (strains WH-I, Bang373, Cal-1, and IDIR) and two C-VP1 (strains Bristol and Cowden) sequences are known (2,5,7,14,26,45). The VP1 sequences from strains J19 and B219 are closely related to those of B-VP1 but form a separate, distinct branch, consistent with their classification into a novel RV group (Fig.…”

Section: Genetic Variation Among Group a B And C Rv Rdrpsmentioning

confidence: 99%

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Shared and Group-Specific Features of the Rotavirus RNA Polymerase Reveal Potential Determinants of Gene Reassortment Restriction

McDonald

Aguayo

González‐Nilo

et al. 2009

J Virol

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Rotaviruses (RVs) are nonenveloped, 11-segmented, double-stranded RNA viruses that are major pathogens associated with acute gastroenteritis. Group A, B, and C RVs have been isolated from humans; however, intergroup gene reassortment does not occur for reasons that remain unclear. This restriction might reflect the failure of the viral RNA-dependent RNA polymerase (RdRp; VP1) to recognize and replicate the RNA of a different group. To address this possibility, we contrasted the sequences, structures, and functions of RdRps belonging to RV groups A, B, and C (A-VP1, B-VP1, and C-VP1, respectively). We found that conserved amino acid residues are located within the hollow center of VP1 near the active site, whereas variable, group-specific residues are mostly surface exposed. By creating a three-dimensional homology model of C-VP1 with the A-VP1 crystallographic data, we provide evidence that these RV RdRps are nearly identical in their tertiary folds and that they have the same RNA template recognition mechanism that differs from that of B-VP1. Consistent with the structural data, recombinant A-VP1 and C-VP1 are capable of replicating one another's RNA templates in vitro. Nonetheless, the activity of both RdRps is strictly dependent upon the presence of cognate RV core shell protein A-VP2 or C-VP2, respectively. Together, the results of this study provide unprecedented insight into the structure and function of RV RdRps and support the notion that VP1 interactions may influence the emergence of reassortant viral strains.

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Section: Genetic Variation Among Group a B And C Rv Rdrpssupporting

confidence: 58%

Section: Genetic Variation Among Group a B And C Rv Rdrpsmentioning

confidence: 99%

Shared and Group-Specific Features of the Rotavirus RNA Polymerase Reveal Potential Determinants of Gene Reassortment Restriction

McDonald

Aguayo

González‐Nilo

et al. 2009

J Virol

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“…Bremont et al [4] have recently shown by sequencing genes 1-4 of group C rotavirus, that. the fourth largest protein with a mol.…”

Section: Discussionmentioning

confidence: 98%

“…As seen in Table t the 78 kD protein is the fourth largest and may be equivalent to the 83kD identified by Bremont etal. [4]. The 78kD structural polypeptide was only detected in infected cell lysates where the AmC-1 virus analysed had been propagated in the absence of trypsin and harvested in the presence of protease inhibitors.…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis and morphogenesis of group C rotavirus in swine testicular cells

Nilsson

Bonsdorff

Svensson

1993

Archives of Virology

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Summary. Polypeptide synthesis and morphogenesis of a group C rotavirus (AmC-1) adapted to a continuous swine testicular cell line was examined. SDS-PAGE analysis of 35 S methionine labeled infected cell lysates revealed 9 viral polypeptides (122, 98, 79, 78, 43, 41, 35, 24, and 20kD). Viral polypeptide synthesis appeared to be maximal at 7-10h post infection. Purified group C virus grown in the presence of trypsin was found to contain seven structural polypeptides (122, 98, 79, 53, 43, 41, and 30kD) by protein blotting and five polypeptides (98, 79, 78, 43, and 41 kD) by immunoprecipitation with a hyperimmune rabbit antisera. Tunicamycin treatment, Concanavalin A binding, protein blotting, endo-H treatment and 2,6 H-mannose labeling suggested that group c rotavirus contains one structural glycoprotein (41 kD) with a corresponding precursor mol. wt. of 37 kD and one not previously identified nonstructural glycoprotein (24 kD) with a corresponding precursor mol. wt. of << 20 kD. Electron microscopy of infected swine testicular cells revealed an assembly process for group C rotavirus similar to group A, with single-shelled particles budding through the rough endoplasmic reticulum with concomitant acquisition of a transient membrane.

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“…To date, the VP1 sequence has been poorly studied; specifically, few amino acids have been suggested to play an important role in protein function. Previous studies include the identification of conserved residues by full sequence alignments of VP1 from group A, B and C rotaviruses (Bremont et al, 1992, Eiden & Hirshon, 1993, Mitchell & Both, 1990, and by short alignments using other viral replicases of positive strand RNA viruses (Cohen et al, 1989, Mitchell & Both, 1990. The function of these conserved amino acids has been described in other viral RNA polymerases (i.e.…”

Section: Introductionmentioning

confidence: 99%

Bioinformatic prediction of polymerase elements in the rotavirus VP1 protein

et al. 2006

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SUMMARYRotaviruses are the major cause of acute gastroenteritis in infants world-wide. The genome consists of eleven double stranded RNA segments. The major segment encodes the structural protein VP1, the viral RNAdependent RNA polymerase (RdRp), which is a minor component of the viral inner core. This study is a detailed bioinformatic assessment of the VP1 sequence. Using various methods we have identified canonical motifs within the VP1 sequence which correspond to motifs previously identified within RdRps of other positive strand, double-strand RNA viruses. The study also predicts an overall structural conservation in the middle region that may correspond to the palm subdomain and part of the fingers and thumb subdomains, which comprise the polymerase core of the protein. Based on this analysis, we suggest that the rotavirus replicase has the minimal elements to function as an RNA-dependent RNA polymerase. VP1, besides having common RdRp features, also contains large unique regions that might be responsible for characteristic features observed in the Reoviridae family.

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Sequences of the four larger proteins of a porcine group C rotavirus and comparison with the equivalent group a rotavirus proteins

Cited by 36 publications

References 37 publications

Shared and Group-Specific Features of the Rotavirus RNA Polymerase Reveal Potential Determinants of Gene Reassortment Restriction

Shared and Group-Specific Features of the Rotavirus RNA Polymerase Reveal Potential Determinants of Gene Reassortment Restriction

Biosynthesis and morphogenesis of group C rotavirus in swine testicular cells

Bioinformatic prediction of polymerase elements in the rotavirus VP1 protein

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