Home About us Contact
|
Home About us Contact | ||
|
|
||
RNA Segment (rna + segment)
Selected AbstractsPurification and characterization of a new reovirus from the Chinese mitten crab, Eriocheir sinensisJOURNAL OF FISH DISEASES, Issue 12 2004S Zhang Abstract A new reovirus was recently isolated from a freshwater crab, the Chinese mitten crab, Eriocheir sinensis, in China. The complete viral particles are 55 nm in diameter, icosahedral, non-enveloped and have a mean buoyant density of 1.39 g cm,3 in CsCl gradient. The viral genome is composed of 12 pieces of dsRNA with an electrophoretic pattern of 3/4/2/3. This virus infects connective tissue of the gills, gut and hepatopancreas. Partial cDNA cloning and sequence analysis showed that the RNA-dependent RNA polymerase is located in the first RNA segment. From its biochemical, ultrastructural and physicochemical properties, this virus is quite different from the genus Aquareovirus (Reoviridae). It may represent a new genus of Reoviridae, different from the other crab reoviruses, P and W2. [source] Genetic characterization of the M RNA segment of a Balkan Crimean-Congo hemorrhagic fever virus strain,JOURNAL OF MEDICAL VIROLOGY, Issue 3 2005Anna Papa Abstract Crimean-Congo hemorrhagic fever (CCHF) virus causes one of the most severe diseases in humans, with a mortality rate of up to 30%. It is transmitted to humans by the bite of hard ticks or by contact with blood or tissues from human patients or infected livestock. Balkan Peninsula is an endemic region of the disease, and sporadic cases or even outbreaks are observed every year. The M RNA segment encodes for the glycoprotein precursor of two surface glycoproteins Gn and Gc. Up to now complete M RNA CCHF virus sequences have been published from strains isolated in Nigeria, China, Pakistan, Tajikistan, and Russia. In the present study, the genetic characterization of the complete nucleotide sequence of the M RNA segment of a Balkan CCHF virus strain, Kosovo/9553/2001, isolated in summer of 2001 from a human fatal case in Kosovo is reported. This is the first published complete M nucleotide sequence of a CCHF virus strain isolated in Balkans. It was found that the Balkan strain is similar to the Russian strain, both strains differing from all other completely sequenced CCHF virus strains by approximately 22% at the nucleotide level forming an independent clade in the phylogenetic tree. J. Med. Virol. 75:466,469, 2005. © 2005 Wiley-Liss, Inc. [source] Full genomic amplification and subtyping of influenza A virus using a single set of universal primersMICROBIOLOGY AND IMMUNOLOGY, Issue 3 2010Emi Inoue ABSTRACT Influenza A virus has eight-segmented RNA molecules as a genome and, among all strains of the virus, both ends of each segment have 13 and 12 nucleotide sequences conserved. In the present study, a simple RT-PCR method to amplify all eight segments of the virus and determine the HA and NA subtype using a single primer set based on the conserved terminal sequences has been established. This method is also capable of detecting subgenomic defective interfering RNA of the influenza A virus. Since the primers used here cope with each and every RNA segment of influenza A virus, this simple RT-PCR method is valuable not only for cloning each gene of the virus, but also for identifying subtypes, including subtypes other than 16 HA and 9 NA subtypes. [source] Mammalian reovirus core protein,µ2 initiates at the first start codon and is acetylatedRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 24 2002Magdalena I. Swanson Mammalian reovirus is an enteric virus that contains a double-stranded RNA genome. The genome consists of ten RNA segments that encode eight structural and three non-structural proteins. The structural proteins form a double-layered structure. The innermost layer, called the core, consists of five proteins (,1, ,2, ,3, µ2, and ,2). Protein ,3 is the RNA-dependent RNA polymerase (RdRp) and µ2 is thought to be an RdRp cofactor. Translation of most reovirus proteins is known to commence at the first start codon. However, the translation initiation site of the viral core protein,µ2, encoded by the M1 RNA segment, has been in dispute. Although the theoretical molecular weight of µ2 is 83 267,Da the actual molecular weight is unknown because,µ2 runs aberrantly in SDS-PAGE and has resisted characterization by Edman degradation, indicating that the amino terminus is post-translationally modified. In this study, we used proteolysis coupled with MALDI-Qq-TOFMS to determine that translation of µ2 initiates at the first AUG codon, that its actual molecular weight approximates the theoretical value of 83,kDa, that the amino terminal methionine residue is removed, and that the next amino acid (alanine) is post-translationally acetylated. Copyright © 2002 John Wiley & Sons, Ltd. [source] Protein structure preference, tRNA copy number, and mRNA stem/loop contentBIOPOLYMERS, Issue 6 2004Liaofu Luo Abstract From statistical analyses of protein sequences for humans and Escherichia coli we found that the messenger RNA segment of m -codons (for m=2 to 6) with average high tRNA copy number (TCN) (larger than ,10.5 for humans or ,1.95 for E. coli) preferably code for the , helix and that with low TCN (smaller than ,7.5 for humans or ,1.7 for E. coli) preferably code for coil. Between them there is an intermediate region without correlation to structure preference. For the , strand the preference/ avoidance tendency is not obvious. All strong preference-modes of TCN for protein secondary structures have been deduced. The mutual interaction between two factors,protein secondary structural type and codon TCN,is tested by F distribution. A phenomenological model on the relation between structure preference and translational efficiency or accuracy is proposed. It is pointed out that the structure preference of codons is related to the distribution of mRNA stem/loop content in three TCN regions. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004 [source] Sequence analysis of genes encoding structural and nonstructural proteins of a human group B rotavirus detected in Calcutta, IndiaJOURNAL OF MEDICAL VIROLOGY, Issue 4 2001Nobumichi Kobayashi Abstract Nucleotide sequences of RNA segments encoding structural proteins(VP4, VP6, and VP7) and nonstructural proteins(NSP1 and NSP3) of a human group B rotavirus CAL-1, which was detected in Calcutta, India, were determined and their relatedness with cognate genes of other group B rotaviruses was analyzed. The CAL-1 genes showed generally high sequence identities (more than 90%) to those of human group B rotavirus, adult diarrheal rotavirus (ADRV) in China, while identities with bovine, murine, and ovine viruses were considerably lower (58,73%). Among RNA segments analyzed, sequence identity of the VP6 gene was relatively high compared with other gene segments. In the CAL-1 VP7 sequence, many characteristics were shared by ADRV, but not by other animal group B rotaviruses. In contrast, VP4 and NSP3 of CAL-1 were single animo acid and 23 amino acids longer than those of ADRV strain, respectively, due to differences of a few nucleotides. These findings suggested that human group B rotaviruses CAL-1 and ADRV might have originated from a common ancestral virus distinct from animal group B rotaviruses reported so far, while some notable sequence differences indicated the distinct nature of these viruses. J. Med. Virol. 64:583,588, 2001. © 2001 Wiley-Liss, Inc. [source] Mammalian reovirus core protein,µ2 initiates at the first start codon and is acetylatedRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 24 2002Magdalena I. Swanson Mammalian reovirus is an enteric virus that contains a double-stranded RNA genome. The genome consists of ten RNA segments that encode eight structural and three non-structural proteins. The structural proteins form a double-layered structure. The innermost layer, called the core, consists of five proteins (,1, ,2, ,3, µ2, and ,2). Protein ,3 is the RNA-dependent RNA polymerase (RdRp) and µ2 is thought to be an RdRp cofactor. Translation of most reovirus proteins is known to commence at the first start codon. However, the translation initiation site of the viral core protein,µ2, encoded by the M1 RNA segment, has been in dispute. Although the theoretical molecular weight of µ2 is 83 267,Da the actual molecular weight is unknown because,µ2 runs aberrantly in SDS-PAGE and has resisted characterization by Edman degradation, indicating that the amino terminus is post-translationally modified. In this study, we used proteolysis coupled with MALDI-Qq-TOFMS to determine that translation of µ2 initiates at the first AUG codon, that its actual molecular weight approximates the theoretical value of 83,kDa, that the amino terminal methionine residue is removed, and that the next amino acid (alanine) is post-translationally acetylated. Copyright © 2002 John Wiley & Sons, Ltd. [source] | |||||||||||||