Scheme depicting the mechanism of NP internalization. Hydrophilic NPs adsorb to the lipid are wrapped and finally internalized into the fluid liposomes, thereby forming supported lipid bilayer (SLB) NPs (the inset depicts the process of invagination)

A model depicting the function of dynamin in fission (left), and s-Mgm1 in fusion (right). Both dynamin and Mgm1 shape membranes in vivo and in vitro. Dynamin dimers assemble into a helical collar, which upon GTPase activity constrict the underlying membrane to mediate fission. We propose that s-Mgm1 forms a homo-oligomeric complex in trans to create protein bridges and ordered lattices that tether opposing membranes to support mitochondrial inner membrane cristae structures, and to also undergo a GTP-induced transition to promote fusion.

MxA protein interacts with negatively charged round liposomes and transforms them into long helical tubes, displaying a characteristic T- shape structure at the lipid outer surface. MxA is a key component of the innate antiviral response. MxA tubes might act as a stable storage form, from which antivirally active monomers are released.

MxA forms ER-associated homooligomers. Upon infection, MxA monomers are released. MxA monomers form copolymers with the viral NPs and associate them to the ER. Misslocation of the NPs to the ER leads to viral inhibition