共 58 条
Mutational analysis of HIV-2 Vpx shows that proline residue 109 in the poly-proline motif regulates degradation of SAMHD1
被引:10
作者:

Ciftci, Halil Ibrahim
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机构:
Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan

Fujino, Haruna
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Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan

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Yamamoto, Minami
论文数: 0 引用数: 0
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机构:
Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan

Kawamura, Sogo
论文数: 0 引用数: 0
h-index: 0
机构:
Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan

Tateishi, Hiroshi
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h-index: 0
机构:
Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan

Iwatani, Yasumasa
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h-index: 0
机构:
Natl Hosp Org, Nagoya Med Ctr, Clin Res Ctr, Nagoya, Aichi, Japan Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan

Otsuka, Masami
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h-index: 0
机构:
Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan

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机构:
[1] Kumamoto Univ, Fac Life Sci, Dept Bioorgan Med Chem, Kumamoto, Japan
[2] Natl Hosp Org, Nagoya Med Ctr, Clin Res Ctr, Nagoya, Aichi, Japan
[3] Kumamoto Univ, Sch Pharm, Res Inst Drug Discovery, Kumamoto, Japan
基金:
日本学术振兴会;
关键词:
HIV-2;
Vpx;
SAMHD1;
Poly-proline;
IMMUNODEFICIENCY-VIRUS TYPE-1;
AICARDI-GOUTIERES SYNDROME;
RESTRICTION FACTOR SAMHD1;
VIRAL INFECTIVITY;
PROTEIN;
REPLICATION;
GENE;
VIF;
ASSOCIATION;
EXPRESSION;
D O I:
10.1016/j.febslet.2015.04.038
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:
In this study, we performed a mutational analysis to determine whether the mechanism by which HIV-2 Vpx confers the capacity for infectivity and viral replication in macrophages is solely dependent on its ability to degrade the host antiviral factor SAMHD1. Contrary to expectations, we demonstrated that P109 in the C-terminal poly-proline motif of HIV-2 Vpx has two unique roles: to facilitate the specific degradation of SAMHD1 in macrophages, and to facilitate multimerization of Vpx, therefore preventing SAMHD1 degradation in the presence of high levels of Vpx. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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收藏
页码:1505 / 1514
页数:10
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机构: Univ Tokushima, Grad Sch Med, Dept Virol, Tokushima 7708503, Japan

Koyama, AH
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机构: Univ Tokushima, Grad Sch Med, Dept Virol, Tokushima 7708503, Japan

Sakai, K
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机构: Univ Tokushima, Grad Sch Med, Dept Virol, Tokushima 7708503, Japan

Adachi, A
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机构: Univ Tokushima, Grad Sch Med, Dept Virol, Tokushima 7708503, Japan