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      Identification of a novel envelope protein encoded by ORF 136 from Cyprinid herpesvirus 3

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          Abstract

          Cyprinid herpesvirus 3 (CyHV-3) is the pathogenic agent of koi herpesvirus disease (KHVD) afflicting common carp and koi ( Cyprinus carpio L.) populations globally. As described previously, proteomic analyses of purified CyHV-3 particles have shown that at least 46 structural proteins are incorporated into CyHV-3 virions; among these ORF136 may encode a putative envelope protein. In this study, Western blotting analysis showed that a specific band with the predicted molecular weight of 17 kDa was detected both in purified virions and envelope components using a rabbit anti-ORF136 polyclonal antibody. Indirect immunofluorescence assay with confocal laser scanning microscopy indicated that the ORF136 protein was distributed in the cytoplasm of CCB cells infected with CyHV-3 and transfected with a pVAX1-ORF136 plasmid. Furthermore, immunogold electron microscopy confirmed that ORF136 protein localized to the CyHV-3 envelope.

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          Genome sequences of three koi herpesvirus isolates representing the expanding distribution of an emerging disease threatening koi and common carp worldwide.

          Herve Bercovier, Andrew Davison, Avi Eldar … (2007)
          Since the mid-1990s, lethal infections of koi herpesvirus (KHV) have been spreading, threatening the worldwide production of common carp and koi (both Cyprinus carpio). The complete genome sequences of three KHV strains from Japan, the United States, and Israel revealed a 295-kbp genome containing a 22-kbp terminal direct repeat. The finding that 15 KHV genes have clear homologs in the distantly related channel catfish virus (ictalurid herpesvirus 1) confirms the proposed place of KHV in the family Herpesviridae, specifically in the branch with fish and amphibian hosts. KHV thus has the largest genome reported to date for this family. The three strains were interpreted as having arisen from a wild-type parent encoding 156 unique protein-coding genes, 8 of which are duplicated in the terminal repeat. In each strain, four to seven genes from among a set of nine are fragmented by frameshifts likely to render the encoded proteins nonfunctional. Six of the affected genes encode predicted membrane glycoproteins. Frameshifts or other mutations close to the 3' ends of coding sequences were identified in a further six genes. The conclusion that at least some of these mutations occurred in vivo prompts the hypothesis that loss of gene functions might be associated with emergence of the disease and provides a basis for further investigations into the molecular epidemiology of the virus.
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            Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins

            Karthik Sathiyamoorthy, Yao Xiong Hu, Britta S. Möhl … (2016)
            Herpesvirus entry into host cells is mediated by multiple virally encoded receptor binding and membrane fusion glycoproteins. Despite their importance in host cell tropism and associated disease pathology, the underlying and essential interactions between these viral glycoproteins remain poorly understood. For Epstein–Barr virus (EBV), gHgL/gp42 complexes bind HLA class II to activate membrane fusion with B cells, but gp42 inhibits fusion and entry into epithelial cells. To clarify the mechanism by which gp42 controls the cell specificity of EBV infection, here we determined the structure of gHgL/gp42 complex bound to an anti-gHgL antibody (E1D1). The critical regulator of EBV tropism is the gp42 N-terminal domain, which tethers the HLA-binding domain to gHgL by wrapping around the exterior of three gH domains. Both the gp42 N-terminal domain and E1D1 selectively inhibit epithelial-cell fusion; however, they engage distinct surfaces of gHgL. These observations clarify key determinants of EBV host cell tropism.
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              Proteomic analysis of the major envelope and nucleocapsid proteins of white spot syndrome virus.

              Limei Xu, Xixian Xie, Quan-Feng Yang (2006)
              White spot syndrome virus (WSSV) virions were purified from the tissues of infected Procambarus clarkii (crayfish) isolates. Pure WSSV preparations were subjected to Triton X-100 treatment to separate into the envelope and nucleocapsid fractions, which were subsequently separated by 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The major envelope and nucleocapsid proteins were identified by either matrix-assisted laser desorption ionization-time of flight mass spectrometry or defined antibody. A total of 30 structural proteins of WSSV were identified in this study; 22 of these were detected in the envelope fraction, 7 in the nucleocapsid fraction, and 1 in both the envelope and the nucleocapsid fractions. With the aid of specific antibodies, the localizations of eight proteins were further studied. The analysis of posttranslational modifications revealed that none of the WSSV structural proteins was glycosylated and that VP28 and VP19 were threonine phosphorylated. In addition, far-Western and coimmunoprecipitation experiments showed that VP28 interacted with both VP26 and VP24. In summary, the data obtained in this study should provide an important reference for future molecular studies of WSSV morphogenesis.
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                Author and article information

                Contributors
                Qing Wang: sunny_929@163.com
                Sven M. Bergmann: sven.bergmann@fli.bund.de
                Journal
                Journal ID (nlm-ta): Arch Virol
                Journal ID (iso-abbrev): Arch. Virol
                Title: Archives of Virology
                Publisher: Springer Vienna (Vienna )
                ISSN (Print): 0304-8608
                ISSN (Electronic): 1432-8798
                Publication date (Electronic): 16 August 2017
                Publication date PMC-release: 16 August 2017
                Publication date (Print): 2017
                Volume: 162
                Issue: 12
                Pages: 3849-3853
                Affiliations
                [1 ]ISNI 0000 0000 9413 3760, GRID grid.43308.3c, Key Laboratory of Fishery Drug Development of Ministry of Agriculture, Key Laboratory of Aquatic Animal Immune Technology of Guangdong Province, Pearl River Fisheries Research Institute, , Chinese Academy of Fishery Sciences, ; Liwan District, Guangzhou, 510380 People’s Republic of China
                [2 ]ISNI 0000 0000 9833 2433, GRID grid.412514.7, College of Fisheries and Life Science, , Shanghai Ocean University, ; Shanghai, People’s Republic of China
                [3 ]GRID grid.417834.d, German Reference Laboratory for KHVD, Institute of Infectology, Friedrich-Loffler-Institut (FLI), , Federal Research Institute for Animal Health, ; Südufer 10, 17493 Greifswald-Insel Riems, Germany
                Article
                Publisher ID: 3528
                DOI: 10.1007/s00705-017-3528-5
                PMC ID: 5671517
                PubMed ID: 28815395
                SO-VID: 5b081b8b-a7ae-4987-b15d-901e5df8a39f
                Copyright © © The Author(s) 2017
                License:

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

                History
                Date received : 8 May 2017
                Date accepted : 2 August 2017
                Funding
                Funded by: National Science and Technology Pillar Program
                Award ID: 2013BAD12B02
                Award Recipient :
                Funded by: Central Public-interest Scientific Institution Basal Research Fund, CAFS
                Award ID: 2017GH01
                Award Recipient :
                Funded by: Special Scientific Research Funds for Central Non-profit Institutes, Chinese Academy of Fishery Sciences
                Award ID: 2016HY-ZC0601
                Award Recipient :
                Funded by: China Agriculture Research System
                Award ID: CARS-46
                Award Recipient :
                Categories
                Subject: Brief Report
                Custom metadata
                issue-copyright-statement © Springer-Verlag GmbH Austria 2017

                ScienceOpen disciplines: Microbiology & Virology
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology

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