Structural basis on a new potent anti-HIV lectin in complex with oligomannoses of HIV-gp120

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Lectin actinohivin (AH) is expected as a new drug candidate that blocks entry of HIV-1 into human susceptible cells. In order to reveal the structural details of AH in the specific interaction with HMTG protruded from HIV-1 surface, several crystal structures of AH in complex with the targets alpha(1-2)mannobiose and alpha(1-2)mannotriose have been determined by X-ray crystallography.These structures show that alpha(1-2)mannotriose of the principal target adopts a double bracket-shape conformation as a rigid structure, to which AH binds to recognize the target strictly in a Lock-and-Key fashion with so many hydrophobic interactions in addition to the hydrogen bonds. These structural features are useful for developing AH as a more effective antiretroviral drug to suppress the infectious expansion of HIV/AIDS and help expedite an end to the HIV/AIDS pandemic in the near future.