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A novel peptide to disrupt the interaction of BST‐2 and Vpu
Author(s) -
Mi Zeyun,
Wang Xin,
He Yang,
Li Xiaoyu,
Ding Jiwei,
Liu Hongyun,
Zhou Jinming,
Cen Shan
Publication year - 2014
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22488
Subject(s) - tetherin , chemistry , peptide , transmembrane protein , downregulation and upregulation , cell , microbiology and biotechnology , transmembrane domain , cell membrane , stromal cell , biophysics , virology , membrane , viral envelope , biochemistry , biology , cancer research , receptor , gene , glycoprotein
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.