A novel peptide to disrupt the interaction of BST‐2 and Vpu. Issue 3 (May 2014)

• Record Type: Journal Article
• Authors: Mi, Zeyun; Wang, Xin; He, Yang; Li, Xiaoyu; Ding, Jiwei; Liu, Hongyun; Zhou, Jinming; Cen, Shan
• Is Part Of: Biopolymers. Volume 102:Issue 3(2014)
• Page Start: 280
• Page End: 287
• Publication Date: 2014-05
• Subjects: Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.22488
• Languages: English
• ISSNs: 0006-3525

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p>Bone marrow stromal cell antigen 2 (BST‐2) inhibits the release of HIV‐1 and other enveloped viruses from the cell surface. HIV‐1 Vpu binds to BST‐2 through an interaction between transmembrane domains (TMD) of the two proteins and induces the downregulation of cell surface BST‐2, thereby counteracting its antiviral activity. In this study, we designed and prepared a modified peptide BST2‐TM‐P1, which include the sequence of BST‐2 TMD, keeping its property competing with BST‐2 to bind with Vpu. Biological assay results indicate BST2‐TM‐P1 could increase the BST‐2 level at the cell surface in Vpu dependent manner and significantly inhibit the replication of HIV‐1 virion. Our studies indicate that blocking the interaction of Vpu and BST‐2 is an effective way to combat HIV‐1 infection. © 2014 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 280–287, 2014.</p> </abstract>