Identification of a novel secretory leukocyte protease inhibitor-binding protein involved in membrane phospholipid movement

Ching Chung Tseng*, Ching Ping Tseng

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

30 Scopus citations

Abstract

Previous studies have suggested that human salivary secretory leukocyte protease inhibitor (SLPI) inhibits HIV-1 by binding to a host cell surface protein of unknown identity. Using the yeast two-hybrid assay, we identified a gene sequence encoding a novel SLPI-binding protein (SLPI-BP). The 1.5-kb cDNA encodes a 318-amino acid protein with a predicted transmembrane segment near the C-terminus. Sequence analysis revealed that SLPI-BP is the human scramblase protein that is involved in the movement of membrane phospholipids. Co-expression of SLPI and SLPI-BP followed by an S-protein pulldown assay confirmed the specific interaction between these two proteins. Our data represent the first report for the identity of SLPI-BP. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)232-236
Number of pages5
JournalFEBS Letters
Volume475
Issue number3
DOIs
StatePublished - 23 06 2000

Keywords

  • Human immunodeficiency virus
  • Protein-protein interaction
  • Saliva
  • Scramblase
  • Secretory leukocyte protease inhibitor-binding protein

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