Patrice Vende

Institut de Biologie Intégrative de la Cellule

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Didier Poncet

Eurométropole de Strasbourg

Annie Charpilienne

Centre National de la Recherche Scientifique

Matthieu Gratia

Centre National de la Recherche Scientifique

Mariela Duarte

Université Paris-Saclay

Denis Rasschaert

Université de Tours

J. Cohen

Université de Reims Champagne-Ardenne

M. Béarzotti

Virologie et Immunologie Moléculaires

Stéphane Pyronnet

Inserm

ÉS

Émeline Sarot

Université de Toulouse

John T. Patton

Indiana University Bloomington

Cooperative Institutions

Centre National de la Recherche Scientifique

Inserm

Virologie et Immunologie Moléculaires

Institut National de la Recherche Agronomique

Laboratoire de Virologie Moléculaire et Structurale

Université de Toulouse

Université Paris-Sud

Université Paris-Saclay

Centre de Recherche en Cancérologie de Toulouse

Université Toulouse III - Paul Sabatier

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Challenging the Roles of NSP3 and Untranslated Regions in Rotavirus mRNA Translation

PLoS ONE (2016)

Matthieu Gratia Patrice Vende Annie Charpilienne Hilma Carolina Baron Cécile Laroche

Rotavirus NSP3 is a translational surrogate of the PABP-poly(A) complex for rotavirus mRNAs. To further explore the effects of NSP3 and untranslated regions (UTRs) on rotavirus mRNAs translation, we used a quantitative in vivo assay with simultaneous cytoplasmic NSP3 expression (wild-type or deletion mutant) and electroporated rotavirus-like and standard synthetic mRNAs. This assay shows that the last four GACC nucleotides of viral mRNA are essential for efficient translation and that both the NSP3 eIF4G- and RNA-binding domains are required. We also show efficient translation of rotavirus-like mRNAs even with a 5'UTR as short as 5 nucleotides, while more than eleven nucleotides are required for the 3'UTR. Despite the weak requirement for a long 5'UTR, a good AUG environment remains a requirement for rotavirus mRNAs translation.

EIF4G

Eukaryotic translation

10.1371/journal.pone.0145998

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Citations (19)

Two proline residues are essential in the calcium-binding activity of rotavirus VP7 outer capsid protein

Journal of Virology (1997)

Rodrigo Gajardo Patrice Vende Didier Poncet J. Cohen

Rotavirus maturation and stability of the outer capsid are calcium-dependent processes. It has been shown previously that the concentration of Ca2+-solubilizing outer capsid proteins from rotavirus particles is dependent on the virus strain. This property of viral particles has been associated with the gene coding for VP7 (gene 9). In this study the correlation between VP7 and resistance to low [Ca2+] was confirmed by analyzing the origin of gene 9 from reassortant viruses prepared under the selective pressure of low [Ca2+]. After chemical mutagenesis, we selected mutant viruses of the bovine strain RF that are more resistant to low [Ca2+]. The genes coding for the VP7 proteins of these independent mutants have been sequenced. Sequence analysis confirmed that these mutants are independent and revealed that all mutant VP7 proteins have proline 75 changed to leucine and have an outer capsid that solubilized at low [Ca2+]. The mutation of proline 279 to serine is found in all but two mutants. The phenotype of mutants having a single proline change can be distinguished from the phenotype of mutants having two proline changes. Sequence analysis showed that position 75 is in a region (amino acids 65 to 78) of great variability and that proline 75 is present in most of the bovine strains. In contrast, proline 279 is in a conserved region and is conserved in all the VP7 sequences in data banks. This region is rich in oxygenated residues that are correctly allocated in the metal-coordinating positions of the Ca2+-binding EF-hand structure pattern, suggesting that this region is important in the Ca2+ binding of VP7.

10.1128/jvi.71.3.2211-2216.1997

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Citations (35)

Nuclear Localization of Cytoplasmic Poly(A)-Binding Protein upon Rotavirus Infection Involves the Interaction of NSP3 with eIF4G and RoXaN

Journal of Virology (2008)

Maya Harb Michelle M. Becker Damien Vitour Carolina Hilma Baron Patrice Vende

Rotavirus nonstructural protein NSP3 interacts specifically with the 3' end of viral mRNAs, with the eukaryotic translation initiation factor eIF4G, and with RoXaN, a cellular protein of yet-unknown function. By evicting cytoplasmic poly(A) binding protein (PABP-C1) from translation initiation complexes, NSP3 shuts off the translation of cellular polyadenylated mRNAs. We show here that PABP-C1 evicted from eIF4G by NSP3 accumulates in the nucleus of rotavirus-infected cells. Through modeling of the NSP3-RoXaN complex, we have identified mutations in NSP3 predicted to interrupt its interaction with RoXaN without disturbing the NSP3 interaction with eIF4G. Using these NSP3 mutants and a deletion mutant unable to associate with eIF4G, we show that the nuclear localization of PABP-C1 not only is dependent on the capacity of NSP3 to interact with eIF4G but also requires the interaction of NSP3 with a specific region in RoXaN, the leucine- and aspartic acid-rich (LD) domain. Furthermore, we show that the RoXaN LD domain functions as a nuclear export signal and that RoXaN tethers PABP-C1 with RNA. This work identifies RoXaN as a cellular partner of NSP3 involved in the nucleocytoplasmic localization of PABP-C1.

EIF4G

Poly(N-isopropylacrylamide)

Eukaryotic translation

10.1128/jvi.00872-08

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Citations (99)

Partial mapping and sequencing of a fish iridovirus genome reveals genes homologous to the frog virus 3 p31, p40 and human eIF2alpha

HAL (Le Centre pour la Communication Scientifique Directe) (1999)

Yanying Yu M. Béarzotti Patrice Vende W. Ahne Michel Brémont

Iridovirus

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Citations (1)

The BamHI fragment 9 of pseudorabies virus contains genes homologous to the UL24, UL25, UL26, and UL 26.5 genes of herpes simplex virus type 1

Virus Research (1996)

Sybille Dezélée Françoise Bras Patrice Vende Brigitte Simonet Xuan T. A. Nguyen

Pseudorabies

Alphaherpesvirinae

10.1016/0168-1702(96)01293-2

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Citations (28)

Sequence variation of the glycoprotein gene identifies three distinct lineages within field isolates of viral haemorrhagic septicaemia virus, a fish rhabdovirus

HAL (Le Centre pour la Communication Scientifique Directe) (1997)

Abdenour Benmansour B. Basurco A.F. Monnier Patrice Vende J.R. Winton

Sequence (biology)

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Citations (15)

Efficient Translation of Rotavirus mRNA Requires Simultaneous Interaction of NSP3 with the Eukaryotic Translation Initiation Factor eIF4G and the mRNA 3′ End

Journal of Virology (2000)

Patrice Vende Maria Piron Nathalie Castagné Didier Poncet

ABSTRACT In contrast to the vast majority of cellular proteins, rotavirus proteins are translated from capped but nonpolyadenylated mRNAs. The viral nonstructural protein NSP3 specifically binds the 3′-end consensus sequence of viral mRNAs and interacts with the eukaryotic translation initiation factor eIF4G. Here we show that expression of NSP3 in mammalian cells allows the efficient translation of virus-like mRNA. A synergistic effect between the cap structure and the 3′ end of rotavirus mRNA was observed in NSP3-expressing cells. The enhancement of viral mRNA translation by NSP3 was also observed in a rabbit reticulocyte lysate translation system supplemented with recombinant NSP3. The use of NSP3 mutants indicates that its RNA- and eIF4G-binding domains are both required to enhance the translation of viral mRNA. The results reported here show that NSP3 forms a link between viral mRNA and the cellular translation machinery and hence is a functional analogue of cellular poly(A)-binding protein.

EIF4G

EIF4E

EIF4EBP1

Poly(N-isopropylacrylamide)

Viral structural protein

Eukaryotic translation

Initiation factor

EIF4A1

Eukaryotic initiation factor

10.1128/jvi.74.15.7064-7071.2000

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Citations (182)

European brown hare syndrome virus: molecular cloning and sequencing of the genome

Journal of General Virology (1996)

G Le Gall S. Huguet Patrice Vende Jean-François Vautherot Denis Rasschaert

The genome of the European brown hare syndrome virus (EBHSV), a calicivirus related to rabbit haemorrhagic disease virus (RHDV), was fully sequenced. It was 7442 bases long and contained two ORFs. In RHDV, the 5′ large ORF (ORF1) is predicted to encode a polyprotein precursor to the non-structural and capsid proteins. The small ORF (ORF2) encodes a predicted protein of 12 kDa. Alignment of sequences of EBHSV and RHDV showed 71% nucleotide identity; the changes were uniformly scattered over the whole genome. Minor differences could be detected when comparing two EBHSV sequences, indicating that EBHSV could vary to the same extent as RHDV. Four cleavage sites previously identified on the RHDV polyprotein were conserved in EBHSV. These sequencing data clearly show that EBHSV and RHDV share a similar genomic organization and confirm that EBHSV and RHDV are two distinct members within the family Caliciviridae.

ORFS

Caliciviridae

Genomic Organization

Cloning (programming)

10.1099/0022-1317-77-8-1693

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Citations (59)

Épidémiologie moléculaire des rotaviroses bovines en région charolaise

HAL (Le Centre pour la Communication Scientifique Directe) (1999)

Patrice Vende R. Karoum Guislain Manet Claude Rizet F. Schelcher

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