Bifunctional CD4-DC-SIGN Fusion Proteins Demonstrate Enhanced Avidity to gp120 and Inhibit HIV-1 Infection and Dissemination

Du, T., et al., 56(9), 4640-9, Antimicrobial Agents and Chemotherapy, 2012

Direct binding analysis of gp120 protein to CD4-linker-DC SIGN fusion proteins (CLD) was performed using the Octet RED system. Biotinylated gp120 was immobilized onto a Streptavidin biosensor and interactions with the CLDs were characterized. The results indicated that CLDs interacted with gp120 in a bivalent manner. The strongest binding affinity of CLDs to gp120 was achieved with a 35AA linker; shorter linkers potentially hindered the interactions.

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