Results 1 - 10
of
20
Virus-encoded proteinases and proteolytic processing in the Nidovirales
- J. Gen. Virol
, 2000
"... On the basis of similarities in their genome organization and replication strategy, RNA viruses can now be classified into ‘supergroups ’ that often include both animal and plant ..."
Abstract
-
Cited by 105 (29 self)
- Add to MetaCart
(Show Context)
On the basis of similarities in their genome organization and replication strategy, RNA viruses can now be classified into ‘supergroups ’ that often include both animal and plant
The genome organization of the Nidovirales: similarities and differences between arteri-, toro-, and coronaviruses
- Semin Virol
, 1997
"... Viruses in the families Arteriviridae and Coronaviridae have enveloped virions which contain nonseg-mented, positive-stranded RNA, but the constituent genera differ markedly in genetic complexity and virion structure. Nevertheless, there are striking resemblances among the viruses in the organizatio ..."
Abstract
-
Cited by 49 (11 self)
- Add to MetaCart
(Show Context)
Viruses in the families Arteriviridae and Coronaviridae have enveloped virions which contain nonseg-mented, positive-stranded RNA, but the constituent genera differ markedly in genetic complexity and virion structure. Nevertheless, there are striking resemblances among the viruses in the organization and expression of their genomes, and sequence conservation among the polymerase polyproteins strongly suggests that they have a common ancestry. On this basis, the International Committee on Taxonomy of Viruses recently established a new order, Nidovirales, to contain the two families. Here, the common traits and distinguishing features of the Nidovirales are reviewed. r 1997 Academic Press KEY WORDS: arterivirus; coronavirus; torovirus; polyprotein processing; RNA recombination.
Porcine reproductive and respiratory syndrome virus comparison: divergent evolution on two continents
- J
, 1999
"... This article cites 64 articles, 31 of which can be accessed free ..."
Abstract
-
Cited by 47 (7 self)
- Add to MetaCart
(Show Context)
This article cites 64 articles, 31 of which can be accessed free
Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases
- Journal of Virology
, 2000
"... This article cites 61 articles, 35 of which can be accessed free ..."
Abstract
-
Cited by 15 (12 self)
- Add to MetaCart
This article cites 61 articles, 35 of which can be accessed free
Genome of invertebrate iridescent virus type 3 (mosquito iridescent virus
- J. Virol. 2006
"... Updated information and services can be found at: ..."
(Show Context)
Cell Host & Microbe
, 2007
"... See next page for additional authors Follow this and additional works at: ..."
Abstract
- Add to MetaCart
(Show Context)
See next page for additional authors Follow this and additional works at:
BY
, 2014
"... This Dissertation is brought to you for free and open access by the Theses and Dissertations at Loyola eCommons. It has been accepted for inclusion in Dissertations by an authorized administrator of Loyola eCommons. For more information, please contact ecommons@luc.edu. ..."
Abstract
- Add to MetaCart
This Dissertation is brought to you for free and open access by the Theses and Dissertations at Loyola eCommons. It has been accepted for inclusion in Dissertations by an authorized administrator of Loyola eCommons. For more information, please contact ecommons@luc.edu.
The Cysteine Protease Domain of Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 2 Possesses
, 2010
"... Porcine reproductive and respiratory syndrome (PRRS) virus nonstructural protein 2 (nsp2) contains a cysteine protease domain at its N terminus, which belongs to the ovarian tumor (OTU) protease family. In this study, we demonstrated that the PRRSV nsp2 OTU domain antagonizes the type I interferon i ..."
Abstract
- Add to MetaCart
(Show Context)
Porcine reproductive and respiratory syndrome (PRRS) virus nonstructural protein 2 (nsp2) contains a cysteine protease domain at its N terminus, which belongs to the ovarian tumor (OTU) protease family. In this study, we demonstrated that the PRRSV nsp2 OTU domain antagonizes the type I interferon induction by interfering with the NF-B signaling pathway. Further analysis revealed that the nsp2 OTU domain possesses ubiquitin-deconjugating activity. This domain has the ability to inhibit NF-B activation by interfering with the polyubiquitination process of IB, which subsequently prevents IB degradation. To determine whether the nsp2 protein antagonist function can be ablated from the virus, we introduced point mutations into the OTU domain region by use of reverse genetics. The D458A, S462A, and D465A mutations targeting on a B-cell epitope in the OTU domain region generated the viable recombinant viruses, and the S462A and D465A mutants were attenuated for growth in cell culture. The OTU domain mutants were examined to determine whether mutations in the nsp2 OTU domain region altered virus ability to inhibit NF-B activation. The result showed that certain mutations lethal to virus replication impaired the ability of nsp2 to inhibit NF-B activation but that the viable recombinant viruses, vSD-S462A and vSD-D465A, were unable to inhibit NF-B activation as effectively as the wild-type virus. This study represents a fundamental step in elucidating the role of nsp2 in PRRS pathogenesis and provides an important insight in future modified live-virus vaccine
Recommended Citation Zhang, Jianqiang, "PERMISSIVENESS OF SELECTED CELL LINES TO EQUINE ARTERITIS VIRUS: ESTABLISHMENT,
, 2005
"... The Graduate School University of Kentucky 2005 ..."
THE APPLICATION OF A PRRSV REVERSE GENETIC SYSTEM FOR THE STUDY OF NONSTRUCTURAL PROTEIN (NSP) FUNCTION
"... Infectious cDNA clones of PRRSV make it possible to construct marker viruses for the study of virus replication and pathogenesis. The nonstructural protein 2 (nsp2) of porcine reproductive and respiratory syndrome virus (PRRSV) is the single largest protein produced during virus replication. The cDN ..."
Abstract
- Add to MetaCart
(Show Context)
Infectious cDNA clones of PRRSV make it possible to construct marker viruses for the study of virus replication and pathogenesis. The nonstructural protein 2 (nsp2) of porcine reproductive and respiratory syndrome virus (PRRSV) is the single largest protein produced during virus replication. The cDNA of the pCMV-129 infectious PRRSV clone was modified by creating unique Mlu I and SgrA I restrictions sites at nucleotide (nt) positions 3,219 and 3,614, respectively: both located within the C-terminal region of nsp2. cDNAs coding for oligo- and polypeptide tags, including FLAG, enhanced green fluorescent protein (EGFP) and firefly luciferase were inserted into the newly created restriction sites. The results showed that only the EGFP-containing genomes were properly expressed and produced virus. EGFP fluorescence, but not EGFP immunoreactivity, was lost during passage of recombinant EGFP viruses in culture. Sequencing of a fluorescence-negative EGFP virus showed that the EGFP remained intact, except for the appearance of mutations that may affect chromophore formation. The results show that nsp2 can be a site for the expression of foreign proteins. Removal of the region between Mlu I and SgrA I sites resulted in a virus that contained a 131 amino acid deletion. The deleted region was replaced with EGFP or an eight amino acid influenza hemagglutanin (HA) tag. Recombinant viruses were used to infect pigs. Gross and micro-histopathology showed reduced pathogenesis when compared to the parent wild-type virus. The 131 amino acid peptide, when expressed as a recombinant protein and coated onto enzyme linked immunosorbent assay (ELISA) plates, was recognized by sera from pigs infected with wild-type virus, but not the deletion mutants. The results from this study show that nsp2 is a potential target for the development of marker vaccines that can differentiate infected from vaccinated animals (DIVA) and for virus attenuation. THE APPLICATION OF A PRRSV REVERSE GENETIC SYSTEM FOR THE STUDY