作者:Eva Rivero-Buceta、Paula Carrero、Elena Casanova、Elisa G. Doyagüez、Andrés Madrona、Ernesto Quesada、María Jesús Peréz-Pérez、Raquel Mateos、Laura Bravo、Leen Mathys、Sam Noppen、Evgeny Kiselev、Christophe Marchand、Yves Pommier、Sandra Liekens、Jan Balzarini、María José Camarasa、Ana San-Félix
DOI:10.1016/j.ejmech.2015.10.027
日期:2015.12
The glycoprotein gp120 of the HIV-1 viral envelope has a high content in mannose residues, particularly alpha-1,2-mannose oligomers. Compounds that interact with these high-mannose type glycans may disturb the interaction between gp120 and its (co)receptors and are considered potential anti-HIV agents. Previously, we demonstrated that a tripodal receptor (1), with a central scaffold of 1,3,5-triethylbenzene substituted with three 2,3,4-trihydroxybenzoyl groups, selectively recognizes alpha-1,2-mannose polysaccharides. Here we present additional studies to determine the anti-HIV-1 activity and the mechanism of antiviral activity of this compound. Our studies indicate that 1 shows anti-HIV-1 activity in the low micromolar range and has pronounced gp120 binding and HIV-1 integrase inhibitory capacity. However, gp120 binding rather than integrase inhibition seems to be the primary mechanism of antiviral activity of 1. (C) 2015 Elsevier Masson SAS. All rights reserved.