During the replication cycle of double-stranded (ds) RNA viruses, the viral RNA-dependent RNA polymerase (RdRP) replicates and transcribes the viral genome from within the viral capsid. How the RdRP molecules are packaged within the virion and how they function within the confines of an intact capsid are intriguing questions with answers that most likely vary across the different dsRNA virus families. In this study, we have determined a 2.4 Å resolution structure of an RdRP from the human picobirnavirus (hPBV). In addition to the conserved polymerase fold, the hPBV RdRP possesses a highly flexible 24 amino acid loop structure located near the C-terminus of the protein that is inserted into its active site. In vitro RNA polymerization assays and site-directed mutagenesis showed that: (1) the hPBV RdRP is fully active using both ssRNA and dsRNA templates; (2) the insertion loop likely functions as an assembly platform for the priming nucleotide to allow de novo initiation; (3) RNA transcription ...
Emerging viral infections can be identified by using a viral metagenomics approach for clinical human material. Diarrhea samples of patients with unexplained gastroenteritis from the Netherlands were analyzed by using viral metagenomics. Novel circular DNA viruses, bufaviruses, and genogroup III picobirnaviruses were identified. These data expand our knowledge of the human virome.
ID JX310368; SV 1; linear; genomic RNA; STD; VRL; 840 BP. XX AC JX310368; XX DT 30-SEP-2012 (Rel. 114, Created) DT 30-SEP-2012 (Rel. 114, Last updated, Version 1) XX DE Podosphaera partitivirus ptbx-09 RNA-dependant RNA polymerase (RdRp) gene, DE partial cds. XX KW . XX OS Podosphaera partitivirus ptbx-09 OC Viruses; dsRNA viruses; Partitiviridae; unclassified Partitiviridae. XX RN [1] RP 1-840 RA Arous S., Marais A., Faure C., Svanella-Dumas L., Candresse T.; RT Partial sequence of a new Partitivirus infecting Podosphaera tridactyla, RT the Prunus powdery mildew agent; RL Unpublished. XX RN [2] RP 1-840 RA Arous S., Marais A., Faure C., Svanella-Dumas L., Candresse T.; RT ; RL Submitted (12-JUL-2012) to the INSDC. RL Universite de Bordeaux, UMR 1332 Biologie du Fruit et Pathologie, Institut RL National de la Recherche Agronomiques, 71, Avenue Edouard Boulraux, RL Villenave dOrnon, Gironde 33140, France XX DR MD5; e4b67d42714ddc841a3709230431d98c. XX CC ##Assembly-Data-START## CC Sequencing ...
TY - JOUR. T1 - First report of a novel alphapartitivirus in the basidiomycete Rhizoctonia oryzae-sativae. AU - Das, Subha. AU - Das, Sampa. PY - 2019/3/1. Y1 - 2019/3/1. N2 - Rhizoctonia oryzae-sativae is a soil-borne basidiomycete fungus that causes aggregate sheath spot disease on rice worldwide. Here, we report the complete genome sequence of a partitivirus designated as Rhizoctonia oryzae-sativae partitivirus 1 (RosPV1) infecting this fungus. The genome of RosPV1 consists of two double-stranded RNA (dsRNA) segments. The larger segment, designated as dsRNA-1 (1,961 bp), contains a single open reading frame (ORF) that encodes a putative polypeptide with a conserved RNA-dependent RNA polymerase (RdRp) domain. The smaller segment, dsRNA-2 (1,819 bp), also has a single ORF, which is predicted to encode the capsid protein (CP). BLAST searches and phylogenetic analyses suggested that RosPV1 is a representative member of a new species within the genus Alphapartitivirus. This is the first report of ...
Author: Walz, J. et al.; Genre: Journal Article; Published in Print: 1999; Keywords: Electron microscopy; Icosahedral capsids; Image analysis; Thermoplasma.; Degradation; Microscopy; Resolution; Products.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.; Title: Capsids of tricorn protease studied by electron cryomicroscopy
Researchers at Osaka University used electron cryomicroscopy (CryoEM) to image essential cardiac muscle components, known as thin filaments, with unprecedented resolution. They also discovered the mechanism by which these filaments regulate heartbeat via cardiac muscle contractions in the presence or absence of calcium ions by changing their conformations.
An electron microscopy technique, where the sample is rapidly cooled to a cryogenic temperature before imaging using a transmission electron microscope....
This site is supported by the Association of Applied Biologists. It was developed and maintained for many years by scientists at Rothamsted Research: John Antoniw (software, databases and web) Mike Adams (taxonomic and sequence data). This project was rebuilt by Xoons Ltd.. ...
TY - JOUR. T1 - Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography. AU - Chiu, Wah. AU - Smith, Thomas. PY - 1994. Y1 - 1994. N2 - The combined use of electron cryomicroscopy and X-ray crystallography has recently provided unprecedented and unique structural information of virus-antibody complexes. Different kinds of viral proteins have been located and identified on the capsid surface, certain residues of the viral proteins involved in antibody interactions have been identified; the elbow angle of bound antibody has been measured; and the mechanism of antibody-mediated neutralization has been elucidated. Within the next few years, this combined methodology should help investigators resolve the structures of large macromolecular assemblies to even higher resolutions.. AB - The combined use of electron cryomicroscopy and X-ray crystallography has recently provided unprecedented and unique structural information of virus-antibody complexes. ...
The Robert P. Apkarian Integrated Electron Microscopy Core (IECM) facility at Cherry Logan Emerson Hall is expanding to the O. Wayne Rollins Research Center, according to Assistant Dean of Research at the Emory University School of Medicine Michael E. Zwick. ... ...
I am the director of the newly founded Ernst-Ruska-Centre 3 for Structural Biology at the Forschungszentrum Jülich. I was a group leader at the EMBL from 2010 - 2018. I got in touch with electron cryomicroscopy by studying amyloid fibrils in the groups of Marcus Fändrich (now in Ulm, Germany) and Niko Grigorieff (now at Janelia Farm, USA).. For my postdoctoral period, I went to the MRC Laboratory of Molecular Biology (Cambridge, UK) to work with Richard Henderson and Roger Williams. In the last few years, we set up a group to study the mechanisms of autophagy by electron cryomicroscopy. Traditionally, I have been interested in the advancement of high-resolution single-particle EM with a particular focus on helical reconstruction. These developments have led to our recent helical processing software package Spring. More recently, we became interested in improving means of cryo-EM map interpretation by atomic models.. ...
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Presence of Norovirus in food can cause viral gasteroenteritis. Recently, lots of reports relating to Norovirus in food have been published. Special attention must be paid to the raw foods as they are not subjected to further heat treatment. In this study, pegaga, kesum, tauge and ulam raja (popular salad vegetables in Malaysia) were investigated for Norovirus. A total of 32 samples from each type of salad vegetables were purchased from local market and analyzed using One-step RT-PCR (Reverse Transcriptase-Polymerase Chain Reaction) for both genogroups namely Norovirus Genogroup I and Genogroup II. Results showed that tauge had the highest contamination with Norovirus Genogroup I (15.6%) comparing to pegaga (9.4%), kesum (12.5%) and ulam raja (0%). Samples were free from Norovirus Genogroup II. The study showed that raw vegetables are high-risk foods and can be contaminated with Norovirus.. ...
SWISS-MODEL Template Library (SMTL) entry for 1uon.1. REOVIRUS POLYMERASE LAMBDA-3 LOCALIZED BY ELECTRON CRYOMICROSCOPY OF VIRIONS AT 7.6-A RESOLUTION