In retroviruses, receptor binding itself can trigger fusion, with temperature and redox conditions also influencing the fusion mechanism [13], [14].
In addition, beside these direct effects due to target antigen binding, mAbs can trigger important immunological effector mechanisms such as ADCC or complement activation that may contribute to the overall therapeutic efficacy.
This manuscript shows that DENV specific antibodies primed on mast cells (MCs), after binding to DENV can trigger MCs to degranulate and lead to the development of vascular leakage in mice.
This may suggest that GSH binding can trigger relatively global conformation adjustment for poplar apo GrxS14.
Moreover, binding of iron can trigger frataxin oligomerization in vitro, a process that was proposed to scavenge toxic iron in a bioavailable form and to be essential for frataxin function [8].
Its binding can trigger mRNA destabilization and/or translational repression, leading to a decrease in the protein encoded by their cognate mRNAs.
Since receptor binding can trigger downstream signaling in the target cell, nanoparticle engagement of membrane receptors can also be used to directly induce biological responses.
In response to this binding, ErbB proteins can trigger many different cell signaling networks.
Nonetheless, VEGF-A binding to VEGFR1 Ig-like domains 2 and 3 can trigger relatively low levels of trans-autophosphorylation on specific VEGFR1 cytoplasmic tyrosine residues Tyr, Tyr, Tyr, Tyr, Tyr, Tyr and Tyr [ 80– 82].
The binding of allergens to specific IgE antibody attached to membrane receptors on mast cells and basophils can trigger the explosive release of potent mediators of inflammation.
