ADS-J1 inhibits HIV-1 entry by interacting with gp120 and does not block fusion-active gp41 core formation.

Authors :: González-Ortega E
Mena MP
Permanyer M
Ballana E
Clotet B
Esté JA
Source :: Antimicrobial agents and chemotherapy [Antimicrob Agents Chemother] 2010 Oct; Vol. 54 (10), pp. 4487-92. Date of Electronic Publication: 2010 Jul 19.
Publication Year :: 2010
Abstract: 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.

Subjects :: Anti-HIV Agents metabolism
Cell Line
Humans
Naphthalenesulfonates metabolism
Triazines metabolism
Anti-HIV Agents pharmacology
HIV Envelope Protein gp120 metabolism
HIV Envelope Protein gp41 metabolism
HIV-1 drug effects
HIV-1 metabolism
Naphthalenesulfonates pharmacology
Triazines pharmacology
Virus Internalization drug effects

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