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Background The HIV-1 viral envelope originates from the cell membrane and contains different cellular proteins such as MHC class I molecules, which play a role in modulating viral infectivity. HLA-C is known to enhance viral infectivity and reduce sensitivity to neutralizing antibodies by inducing gp120/41 conformational changes that may increase fusion efficiency and viral infectivity [1]. In this work we studied the effect of HLA-C on syncytia formation and of its association with the HIV-1 gp120/41 and with the CD4/CCR5 receptors in purified fusion complexes.

HLA-C increases fusion efficiency between the HIV-1 envelope and the cell membrane and is part of the fusion complex