16
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      The effect of glycosylation on cytotoxicity of Ibaraki virus nonstructural protein NS3

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The cytotoxicity of Ibaraki virus nonstructural protein NS3 was confirmed, and the contribution of glycosylation to this activity was examined by using glycosylation mutants of NS3 generated by site-directed mutagenesis. The expression of NS3 resulted in leakage of lactate dehydrogenase to the culture supernatant, suggesting the cytotoxicity of this protein. The lack of glycosylation impaired the transport of NS3 to the plasma membrane and resulted in reduced cytotoxicity. Combined with the previous observation that NS3 glycosylation was specifically observed in mammalian cells (Urata et al., Virus Research 2014), it was suggested that the alteration of NS3 cytotoxicity through modulating glycosylation is one of the strategies to achieve host specific pathogenisity of Ibaraki virus between mammals and vector arthropods.

          Related collections

          Most cited references21

          • Record: found
          • Abstract: found
          • Article: not found

          Expression vector system based on the chicken beta-actin promoter directs efficient production of interleukin-5.

          We examined the promoter activity of the 1.3-kb chicken beta-actin gene sequence located between the 5' flanking region and the proximal region of the second exon. This promoter region showed higher promoter activity than the simian virus 40 (SV40) early promoter or the Rous sarcoma virus (RSV) long terminal repeat (LTR) as assayed by transient lacZ gene expression in mouse L cells. Furthermore, replacement of the 3' splice sequence in this promoter by that derived from the rabbit beta-globin gene resulted in a approximately 2.5-fold enhancement in the synthesis of beta-galactosidase (beta Gal). Introduction of the SV40 origin of DNA replication (ori) into the vector carrying this hybrid promoter, which we designate the AG promoter, markedly enhanced the production of beta Gal in an SV40 T antigen-producing cell, BMT10. We have constructed a useful vector containing the strong AG promoter, several unique restriction sites, a SV40 polyadenylation signal and the SV40 ori for transient expression of cDNA in BMT10 or COS cells. We demonstrate the use of this vector for efficient production of interleukin-5 in BMT10 cells.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Epizootic heamorragic disease.

            Epizootic haemorrhagic disease (EHD) is an infectious non-contagious viral disease transmitted by insects of the genus Culicoides which affects wild and domestic ruminants. The causative agent, the epizootic haemorrhagic disease virus (EHDV), belongs to the family Reoviridae, genus Orbivirus and shares many morphological and structural characteristics with the other members of the genus such as bluetongue, African horse sickness and equine encephalosis viruses. In recent years EHD outbreaks have been reported in countries bordering the European Union. They caused disease in cattle and severe repercussion on the livestock industry of the affected countries. In the light of recent European bluetongue epizootic these events pose an increasing threat to the European Union. This review includes the most recent information regarding the virus and the disease as well as tools for its diagnosis and control. It is our conviction that more attention should be drawn to both EHDV and the disease itself in order to fulfil all these gaps and not to be unprepared in case future possible incursions. Copyright © 2011 Elsevier Ltd. All rights reserved.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags.

              The majority of proteins that traverse the secretory pathway receive asparagine (Asn)-linked glycosylations. Glycans are bulky hydrophilic modifications that serve a variety of structural and functional roles within the cell. Here, we review the recent growing knowledge on the role of Asn-linked glycans as maturation and quality-control protein tags in the early secretory pathway. The carbohydrate composition encodes crucial information about the structure, localization and age of glycoproteins. The "glycan code" is encoded by a series of glycosidases and carbohydrate transferases that line the secretory pathway. This code is deciphered by carbohydrate-binding proteins that possess distinct carbohydrate binding properties and act as molecular chaperones or sorting receptors. These glycosidases and transferases work in concert with resident secretory pathway carbohydrate-binding proteins to form a network that assists in the maturation and trafficking of both native and aberrant glycoproteins within the cell.
                Bookmark

                Author and article information

                Journal
                J Vet Med Sci
                J. Vet. Med. Sci
                JVMS
                The Journal of Veterinary Medical Science
                The Japanese Society of Veterinary Science
                0916-7250
                1347-7439
                16 July 2015
                December 2015
                : 77
                : 12
                : 1611-1616
                Affiliations
                [1) ]Laboratory of Veterinary Hygiene, Joint Faculty of Veterinary Medicine, Yamaguchi University, 1677–1 Yoshida, Yamaguchi 753–0841, Japan
                Author notes
                [* ]Correspondence to: Watanabe, R., Laboratory of Veterinary Hygiene, Joint Faculty of Veterinary Medicine, Yamaguchi University, 1677–1 Yoshida, Yamaguchi 753–0841, Japan. e-mail: r.nabewo@ 123456gmail.com
                Article
                15-0121
                10.1292/jvms.15-0121
                4710717
                26178820
                c5d42eaf-5ff6-41a3-a26b-aeb2f00cac0a
                ©2015 The Japanese Society of Veterinary Science

                This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial No Derivatives (by-nc-nd) License.

                History
                : 04 March 2015
                : 01 July 2015
                Categories
                Virology
                Full Paper

                cytotoxicity,intracellular distribution,ns3 glycosylation,orbivirus

                Comments

                Comment on this article