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David A. Benfield - One of the best experts on this subject based on the ideXlab platform.
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Structural Proteins of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV)
Advances in experimental medicine and biology, 1995Co-Authors: Eric A. Nelson, Jane Christopher-hennings, David A. BenfieldAbstract:PRRSV is a small, enveloped, RNA virus, which is similar to the arteriviruses in morphology, physicochemical properties, nucleotide sequence, genomic organization and replication strategy.1, 2, 3,4 The arteriviruses include lactate dehydrogenase-elevating virus (LDV), equine arteritis virus (EAV) and simian hemorrhagic fever virus (SHFV).5 Sequence information for the VR-2332,6 Lelystad3 and German isolates2 of PRRSV suggests the presence of 6 open reading frames (ORFs) that may code for Structural Proteins. Three putative, Structural Proteins have been identified for the VR-2332 isolate of PRRSV.7 However, additional Structural Proteins may exist and little information is available regarding the biochemical characteristics of these Proteins. Therefore, the purpose of this study was to identify and conduct the initial characterization of the PRRSV Structural Proteins.
Shirley Gillam - One of the best experts on this subject based on the ideXlab platform.
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Molecular biology of rubella virus Structural Proteins
Biochemistry and cell biology = Biochimie et biologie cellulaire, 1994Co-Authors: Shirley GillamAbstract:Rubella virus is a small, enveloped, positive-stranded RNA virus in the Togaviridae family and bears similarities to the prototype alphaviruses in terms of its genome organization and strategy for viral gene expression. Despite being an important human pathogen, the cell biology of rubella virus remains poorly characterized. This review focuses on the molecular biology of rubella virus Structural Proteins, with emphasis on the proteolytic processing and maturation of virus Structural Proteins, the glycosylation requirement for intracellular transport and function of glycoProteins, and the localization of hemagglutinin- and virus-neutralizing epitopes. A number of significant differences between rubella virus and alphavirus Structural protein expression and maturation were discovered.Key words: rubella virus, N-linked glycosylation, epitope mapping, proteolytic processing.
Eric A. Nelson - One of the best experts on this subject based on the ideXlab platform.
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Structural Proteins of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV)
Advances in experimental medicine and biology, 1995Co-Authors: Eric A. Nelson, Jane Christopher-hennings, David A. BenfieldAbstract:PRRSV is a small, enveloped, RNA virus, which is similar to the arteriviruses in morphology, physicochemical properties, nucleotide sequence, genomic organization and replication strategy.1, 2, 3,4 The arteriviruses include lactate dehydrogenase-elevating virus (LDV), equine arteritis virus (EAV) and simian hemorrhagic fever virus (SHFV).5 Sequence information for the VR-2332,6 Lelystad3 and German isolates2 of PRRSV suggests the presence of 6 open reading frames (ORFs) that may code for Structural Proteins. Three putative, Structural Proteins have been identified for the VR-2332 isolate of PRRSV.7 However, additional Structural Proteins may exist and little information is available regarding the biochemical characteristics of these Proteins. Therefore, the purpose of this study was to identify and conduct the initial characterization of the PRRSV Structural Proteins.
Stephen Gillam - One of the best experts on this subject based on the ideXlab platform.
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Expression and characterization of virus-like particles containing rubella virus Structural Proteins.
Journal of Virology, 1994Co-Authors: D Ou, Thomas C Hobman, Stephen GillamAbstract:Abstract Rubella virus (RV) virions contain two envelope glycoProteins (E1 and E2) and a capsid protein (C). Noninfectious RV-like particles (VLPs) containing three Structural Proteins were expressed in a BHK cell line (BHK-24S) by using an inducible promoter. These VLPs were found to resemble RV virons in terms of their size, their morphology, and some biological activities. In immunoblotting studies, VLPs were found to bind similarly to native RV virions with 10 of a panel of 12 RV-specific murine monoclonal antibodies. Immunization of mice with VLPs induced specific antibody responses against RV Structural Proteins as well as virus-neutralizing and hemagglutination-inhibiting antibodies. After immunization of mice with VLPs, in vitro challenge of isolated lymphocytes with inactivated RV and individual RV Structural Proteins stimulated proliferation. Our data suggest the possibility of using VLPs as immunogens for serodiagnostic assays and RV vaccines.
Jane Christopher-hennings - One of the best experts on this subject based on the ideXlab platform.
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Structural Proteins of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV)
Advances in experimental medicine and biology, 1995Co-Authors: Eric A. Nelson, Jane Christopher-hennings, David A. BenfieldAbstract:PRRSV is a small, enveloped, RNA virus, which is similar to the arteriviruses in morphology, physicochemical properties, nucleotide sequence, genomic organization and replication strategy.1, 2, 3,4 The arteriviruses include lactate dehydrogenase-elevating virus (LDV), equine arteritis virus (EAV) and simian hemorrhagic fever virus (SHFV).5 Sequence information for the VR-2332,6 Lelystad3 and German isolates2 of PRRSV suggests the presence of 6 open reading frames (ORFs) that may code for Structural Proteins. Three putative, Structural Proteins have been identified for the VR-2332 isolate of PRRSV.7 However, additional Structural Proteins may exist and little information is available regarding the biochemical characteristics of these Proteins. Therefore, the purpose of this study was to identify and conduct the initial characterization of the PRRSV Structural Proteins.
