Unlike the MBLs, which block HIV only through binding to the glycosylated envelope proteins (gp120 and gp41) of the virus, SBL inhibited HIV at multiple steps of the virus infection/replication cycle.
The finding that HIV-1 itself (possibly through its gp120) can induce a potent antiviral factor (IFN-beta) in macrophages underlines the complex physiological function of these cells in maintaining normal homeostasis in vivo in response to virus infection.
It was shown that the N-glycan environment around well-defined disulphide bridges of gp120 is highly critical to allow efficient viral infection and transmission.
Finally, we demonstrate that the inhibition of virus infection and virus-mediated cell fusion by soluble CD4 proteins depends on their association with gp120 at this binding site.