Heparin enhances the furin cleavage of HIV-1 gp160 peptides

被引：22
|
作者：
Pasquato, A. [1 ,2 ]
Dettin, M. [2 ]
Basak, A. [3 ]
Gambaretto, R. [2 ]
Tonin, L. [2 ]
Seidah, N. G. [1 ]
Di Bello, C. [2 ]
机构：
[1] Clin Res Inst Montreal, Biochem Neuroendocrinol Lab, Montreal, PQ H2W 1R7, Canada
[2] Univ Padua, Dept Chem Proc Engn, I-35131 Padua, Italy
[3] Ottawa Hlth Res Inst, Dis Aging Program, Reg Protein Chem Ctr, Ottawa, ON K1Y 4E9, Canada
来源：
FEBS LETTERS | 2007年 / 581卷 / 30期
基金：
加拿大健康研究院;
关键词：
HIV-1; furin; heparin; glycosaminoglycan; gp160; processing;
D O I：
10.1016/j.febslet.2007.11.050
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Infectious HIV-1 requires gp160 cleavage by furin at the REKR511 down arrow motif (site1) into the gp120/gp41 complex, whereas the KAKR(503) (site2) sequence remains uncleaved. We synthesized 41mer and 51mer peptides, comprising site1 and site2, to study their conformation and in vitro furin processing. We found that, while the previously reported 19mer and 13mer analogues represent excellent in vitro furin substrates, the present extended sequences require heparin for optimal processing. Our data support the hypothesis of a direct binding of heparin with site1 and site2, allowing selective exposure/accessibility of the REKR sequence, which is only then optimally cleaved by furin. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：5807 / 5813
页数：7
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