![]() To obtain highly active pretriggering candidate molecules we carried out a virtual modeling screen for molecules that interact with sialic acid binding site II on HN, which we propose to be the site responsible for activating F. ![]() We previously identified small molecules that interact with HN and induce it to activate F in an untimely fashion, validating a new antiviral strategy. Conformational changes in the F protein and adoption of the postfusion form of the protein prior to receptor engagement of HN at the host cell membrane inactivate the virus. ![]() It is possible to interfere with this process through premature activation of the F protein, distant from the target cell receptor. For proper viral entry to occur, this process must occur when HN is engaged with host cell receptors at the cell surface. The receptor binding protein of parainfluenza virus, hemagglutinin-neuraminidase (HN), is responsible for actively triggering the viral fusion protein (F) to undergo a conformational change leading to insertion into the target cell and fusion of the virus with the target cell membrane. ![]()
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