Expression of HTLV-I Envelope Protein Fused to Hydrophobic Amino-Terminal Peptide of Baculovirus Polyhedrin in Insect Cells and Its Application for Serological Assays

Hiroshi Nyunoya, Kunitada Shimotohno, Tsutomu Ogura, Masayoshi Kikuchi, Hisahiko Iwamoto, Kazuyo Yamashita, Midori Maekawa, Yutaka Takebe, Kikuko Miyamura, Shudo Yamazaki

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Abstract

The envelope of human T-cell leukemia virus type I (HTLV-I) consists of two glycoproteins gp46 and p20E. Recombinant envelope proteins were produced by using an expression vector derived from insect baculovirus, Bombyx mori nuclear polyhedrosis virus. Polyhedrin fusion proteins C182, N147, and N287 contained whole region p20E, C-terminal half of gp46, and almost whole region gp46, respectively. N147 and N287 were suggested to be processed forms resulting from internal cleavage by cellular enzymes. In cultured cells and the insect larvae, C182 and N147 were produced abundantly enough to be purified to homogeneity; however, N287 was produced poorly and not purified. The purified proteins were recognized by HTLV-I-infected human sera and shown to be highly specific antigens for blood screening systems.

Original languageEnglish
Pages (from-to)1311-1321
Number of pages11
JournalAIDS Research and Human Retroviruses
Volume6
Issue number11
DOIs
Publication statusPublished - 1990 Nov

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ASJC Scopus subject areas

  • Immunology
  • Virology
  • Infectious Diseases

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