3 key studies showing us the possible manner in which the COVID mRNA gene injection enhances infectivity of the virus to the vaccinated person; N-terminal domain (NTD) & receptor binding domain (RBD)
by Paul Alexander
I will embed abstracts & highlight key statements; key is that binding to RBD & NTD (especially NTD) changes conformations & enhances infectiousness (binding to NTD changes (unmasks) RBD to 'up & out'
The virus has become largely resistant to the vaccinal antibodies. Full viral immune escape, original antigenic sin (mortal sin) aka immune priming, immune fixation, immune imprinting, immune prejudicing, and antibody-dependent enhancement of infection (ADEI) and disease (ADED). On display.
Liu et al.
‘the Delta variant completely escaped from anti-N-terminal domain (NTD) neutralizing antibodies, while increasing responsiveness to anti-NTD infectivity-enhancing antibodies…BNT162b2-immune sera lost neutralizing activity and enhanced the infectivity. Unique mutations in the Delta NTD were involved in the enhanced infectivity by the BNT162b2-immune sera.’
Fantini et al.
‘enhancing antibodies have a higher affinity for Delta variants than for Wuhan/D614G NTDs. We show that enhancing antibodies reinforce the binding of the spike trimer to the host cell membrane by clamping the NTD to lipid raft microdomains. This stabilizing mechanism may facilitate the conformational change that induces the demasking of the receptor binding domain. As the NTD is also targeted by neutralizing antibodies, our data suggest that the balance between neutralizing and facilitating antibodies in vaccinated individuals is in favor of neutralization for the original Wuhan/D614G strain.’
Liu et al.
‘screened a series of anti-spike monoclonal antibodies from coronavirus disease 2019 (COVID-19) patients and found that some of antibodies against the N-terminal domain (NTD) induced the open conformation of RBD and thus enhanced the binding capacity of the spike protein to ACE2 and infectivity of SARS-CoV-2.’