OK, so if I understand this correctly, they don’t train the immune system to target these sugars, since they’re used by human cells. Instead, they remove them during the vaccine administration so the immune system can train on the bare spike protein. Cool. Now how would this help when new virus copies come in with sugar-coated proteins, some time after the sugar stripping agent is gone from the system?
Yeah I also don’t understand this part. Can the antibodies targeting the bare spike protein attach to it despite the presence of the sugars? Or are there a few spike proteins in the virus which do not have the sugars, not enough to effectively develop antibodies but enough for already existing antibodies to attach to?
I may have missed it in the article, I’m not in life sciences so I don’t have all the prerequisite knowledge for this
Edit: this came out sounding super negative, I’m actually super excited about this development and all I want is to understand a bit better how it works
from what ive gathered from the abstract,t he glycosolation prevents a more robust immune response, less antibody titers, when they removed it they noticed the immune system recognizes the spike proteins more easily so a stronger immune response and more antibody produced, and a longer titre of antibodies.
first when they removed the “glycans” it revealed more of the protein of the virus, so the immune system recognizes different parts or more of it, so stronger and longer last immune response. the conserved parts is the parts of the proteins that dont mutate much so its easier to become immune to it, the sugars originally hid that part.
OK, so if I understand this correctly, they don’t train the immune system to target these sugars, since they’re used by human cells. Instead, they remove them during the vaccine administration so the immune system can train on the bare spike protein. Cool. Now how would this help when new virus copies come in with sugar-coated proteins, some time after the sugar stripping agent is gone from the system?
Yeah I also don’t understand this part. Can the antibodies targeting the bare spike protein attach to it despite the presence of the sugars? Or are there a few spike proteins in the virus which do not have the sugars, not enough to effectively develop antibodies but enough for already existing antibodies to attach to?
I may have missed it in the article, I’m not in life sciences so I don’t have all the prerequisite knowledge for this
Edit: this came out sounding super negative, I’m actually super excited about this development and all I want is to understand a bit better how it works
Yes same, I see they’ve gotten a positive result so I assume there’s a process, I just don’t understand it.
from what ive gathered from the abstract,t he glycosolation prevents a more robust immune response, less antibody titers, when they removed it they noticed the immune system recognizes the spike proteins more easily so a stronger immune response and more antibody produced, and a longer titre of antibodies.
first when they removed the “glycans” it revealed more of the protein of the virus, so the immune system recognizes different parts or more of it, so stronger and longer last immune response. the conserved parts is the parts of the proteins that dont mutate much so its easier to become immune to it, the sugars originally hid that part.