I feel like all the coverage of this leaves out a massive gaping logical hole.
Like anti-venom / anti-bodies are produced by injecting a horse with venom and then collecting the anti-bodies it produces as a result.
In this situation our man Tim is that horse, and he had to inject himself with 900 different venom injections to produce these broad anti-bodies.
Is the plan going forward, to give horses 900 different venom injections to try and recreate this? Is there a synthetic way of making a known anti-body that they’re not mentioning? If there is, then why are we still injecting horses with so much snake venom?
The immune system is super complicated but essentially when an animal or person are exposed to some sort of substance white blood cells sample that compound and create an antibody that is tailored to bind and neutralize it. Different substances range in their ability to induce this response and it often takes repeat exposures to get the titre to high enough levels. So one way or another some sort of animal needs to be exposed to the venom whether it be horse, goat or mouse and we would harvest the antibody for use in emergency situations where we need to immediately reverse the effects of a snake bite.
Another way would be to do this in cell culture but I’m not quite sure how that works, I think thats easier to do when the proteins are directly coded for like insulin or something. You could probably harvest B cell clones that produce the antibody to the venom, make them immortal and harvest it that way but I’m less familiar with that sort of wok so I can’t really comment further.
To produce ABs in cell culture you usually create a hybridoma cell line, by fusing the B-Cell to an immortal tumour cell line (as you postulated). This approach does however require you to identify the cells that produce the proper antibody.
It gets much easier if you know the exact sequence/structure. To learn this (or find a better one) it is also possible to generate libraries of antibody sequences with semi-random hypervariable regions (the part that binds the antibody) using for example phages that will display any protein on their surface area and then measuring the binding affinity! This is called - drum roll - phage display (very creative).
Thanks for the explainer! My lab specializes in IHC so I’m generally familiar with ag-ab interactions but not so much with antibody development. Its fascinating!
I feel like all the coverage of this leaves out a massive gaping logical hole.
Like anti-venom / anti-bodies are produced by injecting a horse with venom and then collecting the anti-bodies it produces as a result.
In this situation our man Tim is that horse, and he had to inject himself with 900 different venom injections to produce these broad anti-bodies.
Is the plan going forward, to give horses 900 different venom injections to try and recreate this? Is there a synthetic way of making a known anti-body that they’re not mentioning? If there is, then why are we still injecting horses with so much snake venom?
The immune system is super complicated but essentially when an animal or person are exposed to some sort of substance white blood cells sample that compound and create an antibody that is tailored to bind and neutralize it. Different substances range in their ability to induce this response and it often takes repeat exposures to get the titre to high enough levels. So one way or another some sort of animal needs to be exposed to the venom whether it be horse, goat or mouse and we would harvest the antibody for use in emergency situations where we need to immediately reverse the effects of a snake bite.
Another way would be to do this in cell culture but I’m not quite sure how that works, I think thats easier to do when the proteins are directly coded for like insulin or something. You could probably harvest B cell clones that produce the antibody to the venom, make them immortal and harvest it that way but I’m less familiar with that sort of wok so I can’t really comment further.
To produce ABs in cell culture you usually create a hybridoma cell line, by fusing the B-Cell to an immortal tumour cell line (as you postulated). This approach does however require you to identify the cells that produce the proper antibody.
It gets much easier if you know the exact sequence/structure. To learn this (or find a better one) it is also possible to generate libraries of antibody sequences with semi-random hypervariable regions (the part that binds the antibody) using for example phages that will display any protein on their surface area and then measuring the binding affinity! This is called - drum roll - phage display (very creative).
Alright, enough trivia for now.
Thanks for the explainer! My lab specializes in IHC so I’m generally familiar with ag-ab interactions but not so much with antibody development. Its fascinating!