Intricate recognition of glycolipid-like compounds by HIV-1 envelope proteins evaluated with surface plasmon resonance imaging

Tomoko Okada, Arisa Kimura, Hiroshi Miura, Toshinori Nishiyama, Masako Mori, Jyunya Suzuki, Masayo Ogiso, Koji Matsuoka, Toshinori Sato, Kenichi Hatanaka, Norihiko Minoura

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Fusion of human immunodeficiency virus (HIV) to the cell membrane occurs by the specific binding of an envelope protein of HIV-1 (gp120 and gp160) and a glycosphingolipid of the cell membrane. In this study, quantitative and array-based affinity evaluation of gp120 and gp160 was performed by surface plasmon resonance (SPR) and the SPR imaging technique using a substrate immobilized with glycolipid-like compounds (Gb3, GM3, and Lac). Quantitative affinity evaluation showed that gp160 specifically bound to Gb3 and Lac compared with GM3, whereas gp120 showed lower binding affinity and specificity. Array-based evaluation showed that gp160 binds to Gb3 more favorably than Lac and GM3.

Original languageEnglish
Pages (from-to)584-592
Number of pages9
JournalJournal of Carbohydrate Chemistry
Volume31
Issue number7
DOIs
Publication statusPublished - 2012 Sep 1

Keywords

  • Carbohydrate
  • Envelope protein
  • Glycolipid-like compound
  • Human immunodeficiency virus (HIV)
  • Surface plasmon resonance (SPR) imaging

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry

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