scholarly journals Ngoye virus: a novel evolutionary lineage within the genus Flavivirus

2006 ◽  
Vol 87 (11) ◽  
pp. 3273-3277 ◽  
Author(s):  
Gilda Grard ◽  
Jean-Jacques Lemasson ◽  
Massamba Sylla ◽  
Audrey Dubot ◽  
Shelley Cook ◽  
...  
Keyword(s):  
Rna Virus ◽  
Structural Genes ◽  
Degenerate Primers ◽  
Newborn Mice ◽  
Replication Complex ◽  
Viral Particles ◽  
The Family ◽  
Intracerebral Infection ◽  
Distinct Phylogenetic Lineage

By using degenerate primers deduced from conserved patterns in the flavivirus polymerase gene, a novel RNA virus was discovered in Rhipicephalus ticks sampled from members of the family Bovidae in Senegal. It was named Ngoye virus (NGOV) after the location from which it was isolated. Viral particles could be observed by electron microscopy, but isolation in vertebrate or invertebrate cell lines or by intracerebral infection of newborn mice remained unsuccessful. This is atypical of recognized arboviruses. The characterization of 4176 nt of the non-structural genes revealed that NGOV is a novel flavivirus species. It forms a distinct phylogenetic lineage related distantly to previously identified members of the genus Flavivirus. Analysis of genetic data suggested that the processing of the NGOV polyprotein and the organization of its replication complex are similar to those of flaviviruses. Together with other recent data, these findings suggest that a large number of viruses related distantly to ‘classical’ arthropod-borne flaviviruses remain to be discovered.

Molecular characterization of a novel mycovirus isolated from Rhizoctonia solani AG-1 IA 9-11

2021 ◽  
Author(s):  
Yang Sun ◽  
Yan qiong Li ◽  
Wen han Dong ◽  
Ai li Sun ◽  
Ning wei Chen ◽  
...  
Keyword(s):  
Rhizoctonia Solani ◽  
Rna Virus ◽  
Dsrna Virus ◽  
Open Reading Frames ◽  
The Family ◽  
Significant Amino Acid Sequence ◽  
Overlapping Open Reading Frames ◽  
Significant Amino Acid ◽  
Reading Frames

Abstract The complete genome of the dsRNA virus isolated from Rhizoctonia solani AG-1 IA 9–11 (designated as Rhizoctonia solani dsRNA virus 11, RsRV11 ) were determined. The RsRV11 genome was 9,555 bp in length, contained three conserved domains, SMC, PRK and RT-like super family, and encoded two non-overlapping open reading frames (ORFs). ORF1 potentially coded for a 204.12 kDa predicted protein, which shared low but significant amino acid sequence identities with the putative protein encoded by Rhizoctonia solani RNA virus HN008 (RsRV-HN008) ORF1. ORF2 potentially coded for a 132.41 kDa protein which contained the conserved motifs of the RNA-dependent RNA polymerase (RdRp). Phylogenetic analysis indicated that RsRV11 was clustered with RsRV-HN008 in a separate clade independent of other virus families. It implies that RsRV11, along with RsRV-HN008 possibly a new fungal virus taxa closed to the family Megabirnaviridae, and RsRV11 is a new member of mycoviruses.

scholarly journals Isolation and Characterization of an Arterivirus Defective Interfering RNA Genome

2000 ◽  
Vol 74 (7) ◽  
pp. 3156-3165 ◽  
Author(s):  
Richard Molenkamp ◽  
Babette C. D. Rozier ◽  
Sophie Greve ◽  
Willy J. M. Spaan ◽  
Eric J. Snijder
Keyword(s):  
Rna Virus ◽  
Equine Arteritis Virus ◽  
Reading Frame ◽  
Isolation And Characterization ◽  
The Family ◽  
Defective Interfering Rna ◽  
Rna Genome ◽  
Interfering Rna ◽  
Discontinuous Transcription

ABSTRACT Equine arteritis virus (EAV), the type member of the family Arteriviridae, is a single-stranded RNA virus with a positive-stranded genome of approximately 13 kb. EAV uses a discontinuous transcription mechanism to produce a nested set of six subgenomic mRNAs from which its structural genes are expressed. We have generated the first documented arterivirus defective interfering (DI) RNAs by serial undiluted passaging of a wild-type EAV stock in BHK-21 cells. A cDNA copy of the smallest DI RNA (5.6 kb) was cloned. Upon transfection into EAV-infected BHK-21 cells, transcripts derived from this clone (pEDI) were replicated and packaged. Sequencing of pEDI revealed that the DI RNA was composed of three segments of the EAV genome (nucleotides 1 to 1057, 1388 to 1684, and 8530 to 12704) which were fused in frame with respect to the replicase reading frame. Remarkably, this DI RNA has retained all of the sequences encoding the structural proteins. By insertion of the chloramphenicol acetyltransferase reporter gene in the DI RNA genome, we were able to delimitate the sequences required for replication/DI-based transcription and packaging of EAV DI RNAs and to reduce the maximal size of a replication-competent EAV DI RNA to approximately 3 kb.

scholarly journals Salicylic Acid Inhibits the Replication of Tomato bushy stunt virus by Directly Targeting a Host Component in the Replication Complex

2015 ◽  
Vol 28 (4) ◽  
pp. 379-386 ◽  
Author(s):  
Miaoying Tian ◽  
Zsuzsanna Sasvari ◽  
Paulina Alatriste Gonzalez ◽  
Giulia Friso ◽  
Elden Rowland ◽  
...  
Keyword(s):  
Salicylic Acid ◽  
Rna Virus ◽  
Tomato Bushy Stunt Virus ◽  
Glycolytic Enzyme ◽  
Replication Complex ◽  
Important Host ◽  
Underlying Mechanisms ◽  
Gapdh Protein

Although the plant hormone salicylic acid (SA) plays a central role in signaling resistance to viral infection, the underlying mechanisms are only partially understood. Identification and characterization of SA’s direct targets have been shown to be an effective strategy for dissecting the complex SA-mediated defense signaling network. In search of additional SA targets, we previously developed two sensitive approaches that utilize SA analogs in conjunction with either a photoaffinity labeling technique or surface plasmon resonance-based technology to identify and evaluate candidate SA-binding proteins (SABPs) from Arabidopsis. Using these approaches, we have now identified several members of the Arabidopsis glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein family, including two chloroplast-localized and two cytosolic isoforms, as SABPs. Cytosolic GAPDH is a well-known glycolytic enzyme; it also is an important host factor involved in the replication of Tomato bushy stunt virus (TBSV), a single-stranded RNA virus. Using a yeast cell-free extract, an in vivo yeast replication system, and plant protoplasts, we demonstrate that SA inhibits TBSV replication. SA does so by inhibiting the binding of cytosolic GAPDH to the negative (−)RNA strand of TBSV. Thus, this study reveals a novel molecular mechanism through which SA regulates virus replication.

scholarly journals Molecular characterization of a porcine sapovirus strain isolated from a piglet with diarrhoea: a case report

2011 ◽  
Vol 56 (No. 8) ◽  
pp. 409-415 ◽  
Author(s):  
L. Dufkova ◽  
P. Kulich ◽  
J. Prodelalova
Keyword(s):  
Czech Republic ◽  
Rna Polymerase ◽  
The Czech Republic ◽  
Porcine Sapovirus ◽  
Viral Particles ◽  
Faecal Samples ◽  
The Family ◽  
Capsid Gene Sequence ◽  
Negative Staining Electron Microscopy

Porcine sapoviruses, members of the family Caliciviridae, have been considered as an aetiological agent of gastroenteritis in pigs. In this study, we analysed 251 faecal samples obtained from 3 to 90 day-old diarrhoeic pigs in the Czech Republic between January 2005 and June 2010 and tested them by negative staining electron microscopy for the presence of sapoviruses. Only one sample showed the presence of viral particles with characteristic sapovirus morphology. The presence of sapovirus (SaV) was confirmed by an RT-PCR assay with primers specific for the sapoviral RNA polymerase and capsid genes. Phylogenetic analysis based on a partial sequence of the RNA polymerase gene placed the new Czech isolate into the GVII genogroup of porcine sapoviruses; however, analysis of a portion of the capsid gene sequence classified the isolate as GIII of the genus Sapovirus. These contradictory findings indicate that recombinant porcine sapovirus was identified. According to our knowledge this is the first description of porcine sapovirus in domestic pigs in the Czech Republic

scholarly journals Analysis of protein–protein interactions in the feline calicivirus replication complex

2006 ◽  
Vol 87 (2) ◽  
pp. 363-368 ◽  
Author(s):  
William J. Kaiser ◽  
Yasmin Chaudhry ◽  
Stanislav V. Sosnovtsev ◽  
Ian G. Goodfellow
Keyword(s):  
Capsid Protein ◽  
Protein Interactions ◽  
Feline Calicivirus ◽  
Protein Protein Interactions ◽  
Replication Complex ◽  
Orf2 Protein ◽  
The Family ◽  
Capsid Protein Vp1 ◽  
The Individual

Caliciviruses are a major cause of gastroenteritis in humans and cause a wide variety of other diseases in animals. Here, the characterization of protein–protein interactions between the individual proteins of Feline calicivirus (FCV), a model system for other members of the family Caliciviridae, is reported. Using the yeast two-hybrid system combined with a number of other approaches, it is demonstrated that the p32 protein (the picornavirus 2B analogue) of FCV interacts with p39 (2C), p30 (3A) and p76 (3CD). The FCV protease/RNA polymerase (ProPol) p76 was found to form homo-oligomers, as well as to interact with VPg and ORF2, the region encoding the major capsid protein VP1. A weak interaction was also observed between p76 and the minor capsid protein encoded by ORF3 (VP2). ORF2 protein was found to interact with VPg, p76 and VP2. The potential roles of the interactions in calicivirus replication are discussed.

scholarly journals Identification and Characterization of a Novel Emaravirus From Grapevine Showing Chlorotic Mottling Symptoms

2021 ◽  
Vol 12 ◽  
Author(s):  
Xudong Fan ◽  
Chen Li ◽  
Zunping Zhang ◽  
Fang Ren ◽  
Guojun Hu ◽  
...  
Keyword(s):  
Phylogenetic Trees ◽  
High Throughput Sequencing ◽  
Rna Virus ◽  
Reading Frame ◽  
A Genome ◽  
The Family ◽  
Pcr Products ◽  
Chlorotic Mottling

A novel negative-sense, single-stranded (ss) RNA virus was identified in a “Shennong Jinhuanghou” (SJ) grapevine showing severe chlorotic mottling symptoms by integrating high-throughput sequencing (HTS) and conventional Sanger sequencing of reverse transcription polymerase chain reaction (RT-PCR) products. The virus was provisionally named as “grapevine emaravirus A” (GEVA). GEVA had a genome comprising five genomic RNA segments, each containing a single open reading frame on the viral complementary strand and two untranslated regions with complementary 13- nt stretches at the 5′ and 3′ terminal ends. RNA1 (7,090 nt), RNA2 (2,097 nt), RNA3 (1,615 nt), and RNA4 (1,640 nt) encoded putative proteins P1–P4 that, based on their conserved motifs, were identified as the RNA-dependent RNA polymerase, glycoprotein, nucleocapsid protein, and movement protein, respectively. However, the functional role of protein P5 encoded by RNA5 (1,308 nt) could not be determined. Phylogenetic trees constructed based on amino acids of P1 to P4, allocated GEVA in clade I, together with other species-related emaraviruses. These data support the proposal that GEVA is a representative member of a novel species in the genus Emaravirus of the family Fimoviridae. Moreover, when GEVA was graft-transmitted to SJ and “Beta” grapevines, all grafted plants showed the same symptoms, similar to those observed in the source of the inoculum. This is the first report to our knowledge of an emaravirus infecting grapevine and its possible association with chlorotic mottling symptoms.

scholarly journals Formation of Disulfide-Linked Complexes between the Three Minor Envelope Glycoproteins (GP2b, GP3, and GP4) of Equine Arteritis Virus

2003 ◽  
Vol 77 (11) ◽  
pp. 6216-6226 ◽  
Author(s):  
Roeland Wieringa ◽  
Antoine A. F. de Vries ◽  
Peter J. M. Rottier
Keyword(s):  
Noncovalent Interactions ◽  
Rna Virus ◽  
Noncovalent Interaction ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Equine Arteritis Virus ◽  
Viral Particles ◽  
The Family ◽  
Infected Cells ◽  
Covalently Linked

ABSTRACT Equine arteritis virus (EAV) is an enveloped, positive-stranded RNA virus belonging to the family Arteriviridae of the order Nidovirales. Six transmembrane proteins have been identified in EAV particles: the nonglycosylated membrane protein M and the glycoprotein GP5 (previously named GL), which occur as disulfide-bonded heterodimers and are the major viral envelope proteins; the unglycosylated small envelope protein E; and the minor glycoproteins GP2b (formerly designated GS), GP3, and GP4. Analysis of the appearance of the GP2b, GP3, and GP4 proteins in viral particles by gel electrophoresis under reducing and nonreducing conditions revealed the occurrence of two different covalently linked oligomeric complexes between these proteins, i.e., heterodimers of GP2b and GP4 and heterotrimers of GP2b, GP3, and GP4. Shortly after their release from infected cells, virions contained mainly cystine-linked GP2b/GP4 heterodimers, which were subsequently converted into disulfide-bonded GP2b/GP3/GP4 trimers through the covalent recruitment of GP3. This process occurred faster at a higher pH but was arrested at 4°C. Furthermore, the conversion was almost instantaneous in the presence of the thiol oxidant diamide. In contrast, the sulfhydryl-modifying agent N-ethylmaleimide inhibited the formation of disulfide-bonded GP2b/GP3/GP4 trimers. Using sucrose density gradients, we could not demonstrate a noncovalent association of GP3 with the cystine-linked GP2b/GP4 dimer in freshly released virions, nor did we observe higher-order structures of the GP2b/GP4 or GP2b/GP3/GP4 complexes. Nevertheless, the instantaneous diamide-induced formation of disulfide-bonded GP2b/GP3/GP4 heterotrimers at 4°C suggests that the three minor glycoproteins of EAV are assembled as trimeric complexes. The existence of a noncovalent interaction between the cystine-linked GP2b/GP4 dimer and GP3 was also inferred from coexpression experiments showing that the presence of GP3 increased the electrophoretic mobility of the disulfide-bonded GP2b/GP4 dimers. Our study reveals that the minor envelope proteins of arteriviruses enter into both covalent and noncovalent interactions, the function of which has yet to be established.

scholarly journals Characterization of Swine Infertility and Respiratory Syndrome (SIRS) Virus (Isolate ATCC VR-2332)

1992 ◽  
Vol 4 (2) ◽  
pp. 127-133 ◽  
Author(s):  
David A. Benfield ◽  
Eric Nelson ◽  
James E. Collins ◽  
Lou Harris ◽  
Sagar M. Goyal ◽  
...  
Keyword(s):  
Virus Isolate ◽  
Rna Virus ◽  
Cesium Chloride ◽  
Average Diameter ◽  
Lactic Dehydrogenase ◽  
Spherical Particles ◽  
Laboratory Studies ◽  
The Family ◽  
Nm Range

The characterization of an isolate of swine infertility and respiratory syndrome (SIRS) virus (ATCC VR-2332) is reported. A commercial cell line (CL262 1) was used for the propagation of the virus for all assays. Laboratory studies indicate that this isolate is a fastidious, nonhemagglutinating, enveloped RNA virus. Cesium chloride-purified virions visualized by electron microscopy were spherical particles with an average diameter of 62 nm (range: 48–83 nm) and a 25–30 nm core surrounded by an envelope. Virus replication was restricted to the cytoplasm, as demonstrated by immunofluorescence. The virus did not react serologically with antisera to several common porcine viruses or with antisera to known viruses in the alphavirus, rubivirus, pestivirus, and ungrouped lactic dehydrogenase virus genera of the Togaviridae. However, convalescent sow sera and rabbit hyperimmune sera neutralized the SIRS virus at titers of 1:256 and 1:512, respectively. The virus was stable at 4 and −70 C, but was labile at 37 and 56 C. The properties of this isolate of SIRS virus resemble those of the family Togaviridae but do not match the described genera.

scholarly journals Identification and Molecular Characterization of a Novel Partitivirus from Trichoderma atroviride NFCF394

Viruses ◽  
2018 ◽  
Vol 10 (11) ◽  
pp. 578 ◽  
Author(s):  
Jeesun Chun ◽  
Han-Eul Yang ◽  
Dae-Hyuk Kim
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Molecular Characteristics ◽  
Trichoderma Atroviride ◽  
Double Stranded Rna ◽  
Reading Frame ◽  
Viral Particles ◽  
The Family ◽  
Isogenic Strains

An increasing number of novel mycoviruses have been described in fungi. Here, we report the molecular characteristics of a novel bisegmented double-stranded RNA (dsRNA) virus from the fungus Trichoderma atroviride NFCF394. We designated this mycovirus as Trichoderma atroviride partitivirus 1 (TaPV1). Electron micrographs of negatively stained, purified viral particles showed an isometric structure approximately of 30 nm in diameter. The larger segment (dsRNA1) of the TaPV1 genome comprised 2023 bp and contained a single open reading frame (ORF) encoding 614 amino acid (AA) residues of RNA-dependent RNA polymerase (RdRp). The smaller segment (dsRNA2) consisted of 2012 bp with a single ORF encoding 577 AA residues of capsid protein (CP). The phylogenetic analysis, based on deduced amino acid sequences of RdRp and CP, indicated that TaPV1 is a new member of the genus Alphapartitivirus in the family Partitiviridae. Virus-cured isogenic strains did not show significant changes in colony morphology. In addition, no changes in the enzymatic activities of β-1,3-glucanase and chitinase were observed in virus-cured strains. To the best of our knowledge, this is the first report of an Alphapartitivirus in T. atroviride.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

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