ADS-J1 Inhibits HIV-1 Entry by Interacting with gp120 and Does Not Block Fusion-Active gp41 Core Formation

被引：19

作者：

Gonzalez-Ortega, Emmanuel ^{[1
]}

Mena, Maria-Pau ^{[1
]}

Permanyer, Marc ^{[1
]}

Ballana, Ester ^{[1
]}

Clotet, Bonaventura ^{[1
]}

Este, Jose A. ^{[1
]}

机构：

[1] Univ Autonoma Barcelona, Hosp Univ Germans Trias & Pujol, Retrovirol Lab IrsiCaixa, Badalona 08916, Spain

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 2010年 / 54卷 / 10期

关键词：

HUMAN-IMMUNODEFICIENCY-VIRUS; SYNCYTIUM-INDUCING PHENOTYPE; ANTI-HIV-1; ACTIVITY; COILED-COIL; SOLUBLE CD4; IN-VITRO; RESISTANCE; TYPE-1; ENVELOPE; GLYCOPROTEIN;

D O I：

10.1128/AAC.00359-10

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

We had shown that virus resistance to ADS-J1 was associated with amino acid changes in the envelope glycoprotein, mostly located in the gp120 coding region. Time-of-addition and endocytic virus transfer assays clearly demonstrated that ADS-J1 behaved as a gp120 inhibitor. ADS-J1-resistant virus was cross-resistant to the polyanion dextran sulfate, and recombination of gp120 recovered only the ADS-J1-resistant phenotype. In summary, ADS-J1 blocks an early step of virus entry that appears to be driven by gp120 alone.

引用

页码：4487 / 4492

页数：6

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