I think I have figured a cure to HIV.

[Kylonicus]

I think I figured out a cure to HIV, basically just create an enzyme which breaks down gp-120 the molecule which attaches to the CD4 receptor.

 

Plus add the enzyme(already been created/researched by somebody else) which removes the sugar molecule from the virus so the gp-120 molecule is accessible.

 

With this one half of the cure and the other half of the cure, you could cure HIV.

 

The gp-120 molecule would all be destroyed, once it was completely destroyed the virus particle would be useless, and thus it would no longer be a threat.

 

Anyway, what do y'all think?

[NPK]

How would you create the enzyme?

[Kylonicus]

Well, one method for creating the enzyme which is being researched by other people right now, is creating a genetic template for it, and inserting into bacteria.

 

The bacteria produce the enzyme, then the enzyme is refined from the bacteria. I don't know how they refine enzymes and chemicals from bacteria, but I know they can, and they do.

 

For instance, CoQ10 that's produced in commercial quantities, produced by this very method. Except I think all they had to do is transfer the genetic material from like an animal, they didn't have to figure out how to genetically encode it.

 

Anyway, just what I am thinking.

[ecoli]

They do this with insulin, and a whole host of other things as well.

[Yggdrasil]

The problem with such a method is that as far as I know, there is no protease which cleaves gp120 in the membrane. As opposed to CoQ, insulin, and other enzymes/proteins produced by biotech companies, there is no gene (template) from which bacteria or other organisms can express the protein. Therefore, one would have to design a novel enzyme from scratch, not an easy task. This has been done by the Hellinga group at Duke, but they designed the enzyme based off of the structure of an already existing enzyme (triosephosphate isomerase). Designing a novel protease for gp120 may be within our capabilities, however, since we do know how many proteases work. The main challenge would be to make the enzyme specific for gp120 in HIV envelope as well as making it stable in the extracellular environment (perhaps something like a catalytic antibody would be suitable as well).

[Kylonicus]

To show my ignorance,

 

I didn't know there were such things as catalytic antibodies, which sound just like enzymes which attack things the body doesn't want.

 

If catalytic antibodies do exist, we could simply use animal(preferablly shark) white blood cells to produce the catalytic antibody to the gp-120 molecule, and of course we'de have to mix in that other enzyme to remove the protective shield of the HIV.

 

Then we could make a hybridoma! Then we'de have a virtually endless supply of HIV medication for people with that disease.

 

Except for the limited supply of the enzyme which removes the sugar molecule.

 

But this way lots of people could be cured.

 

Yahhh!

 

[bascule]

Until the virus evolves a new method for attaching to the CD4 receptor

 

Since HIV is an RNA virus and thus evolves rather quickly, this has been the largest problem with research thus far.

[Yggdrasil]

To show my ignorance' date='

 

I didn't know there were such things as catalytic antibodies, which sound just like enzymes which attack things the body doesn't want.

 

If catalytic antibodies do exist, we could simply use animal(preferablly shark) white blood cells to produce the catalytic antibody to the gp-120 molecule, and of course we'de have to mix in that other enzyme to remove the protective shield of the HIV.

 

Then we could make a hybridoma! Then we'de have a virtually endless supply of HIV medication for people with that disease.

 

Except for the limited supply of the enzyme which removes the sugar molecule.

 

But this way lots of people could be cured.

 

Yahhh!

 

[/quote']

 

Although there are some catalytic antibodies which exist naturally (I believe catalytic antibodies are the cause of lupus), catalytic antibodies are generally created artificially by scientists. So again, you have the problem of engineering an protein, which is not an easy task.

 

Catalytic enzymes basically work by binding the transition state of a reaction. This lowers the activation energy of the reaction and causes it to proceed at a faster rate. They differ from regular enzymes because they have the same structure as an antibody, a hetero-tetramer consisting of two identical light chains and two identical heavy chains in the characteristic "Y" shape of an antibody.