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

FEBS Letters

Tseng, Ching-Chung²  Tseng, Ching-Ping¹ 

[1] School of Medical Technology, Chang Gung University, 259 Wen-Hua 1st Road, Kweishan, Taoyuan, Taiwan;Divisions of Basic Sciences and of Restorative and Prosthodontic Sciences, New York University College of Dentistry, New York, NY 10010, USA

关键词: Secretory leukocyte protease inhibitor-binding protein;    Scramblase;    Saliva;    Human immunodeficiency virus;    Protein–protein interaction;   

DOI  :  10.1016/S0014-5793(00)01700-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown