1
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Baculovirus expression and affinity purification of protein E2 of classical swine fever virus strain Alfort/187.

      Read this article at

      ScienceOpenPublisherPubMed
      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 genome region encoding the major envelope glycoprotein E2 (gp55) of the classical swine fever virus (CSFV) strain Alfort/187 was cloned and sequenced. The E2 gene, either with or without additional authentic 5'-terminal sequences coding for two variants of a putative signal sequence, was used to construct recombinant baculoviruses expressing the respective glycosylated and nonglycosylated E2 protein in insect cells. The signal sequences mediated glycosylation in insect cells, but no efficient secretion of the protein into the cell culture supernatant was observed. Six histidine residues introduced at the carboxy terminus of E2 allowed purification of E2 protein by Ni(2+)-chelate affinity chromatography. The proteins obtained were characterized and their immunological properties were compared by western blot analysis.

          Related collections

          Author and article information

          Journal
          Virus Genes
          Virus genes
          Springer Science and Business Media LLC
          0920-8569
          0920-8569
          1995
          : 10
          : 2
          Affiliations
          [1 ] Institute of Virology and Immunoprophylaxis, Mittelhäusern, Switzerland.
          Article
          10.1007/BF01702592
          8560771
          6ceba236-fe84-4a14-a9ec-b2d30b668d7f
          History

          Comments

          Comment on this article