Over winter break, getting the flu was the talk of the town.
Every pharmacy within a ten-mile radius of me had run out of flu shots, and
people were in a panic on the news. This is supposed to be the worst flu season
ever, and to top it off, the flu season started a few weeks early this year!
The article, “ The Flu’s Proton Escort”, published in
Science Magazine, introduces the structure and significance of the M2 protein.
In the past few flu seasons, researchers have noticed that there is a mutation
in the M2 protein that has made the Influenza virus resistant to two antibiotic
drugs, amantadine and rimantadine. As it is, researchers are always trying to
come up with a new antiviral drug to help fight the virus by trying to predict
the next type of strain. In order to come up with new and better antiviral
drugs, they need to get a better understanding of how the M2 structure reacts
to the drugs.
The M2 gene is a small protein that lets hydrogen ions
access into the viral particle. It mediates
acidification in the interior of the host cell. By changing the pH levels, the
virus RNA is able to easily leave the cell, replicate and spread through your
body. The structure of M2 contains a trans-membrane helix, that mediates drug
binding and channel activity. Because M2 mediates drug binding, it has caused
many debates among researchers as their anti-flu drugs are binding at different
sites. There are two research groups pointed out in this article that did
studies to try and figure out how the M2 is able to do this, and the article
goes more in depth of their tests.
In the end of it all there are still questions about the M2
Protein and researchers are still debating about the correct geometry and
measurements of the side-chain in the M2 structure and all of the tests and
research led to more questions. The flu happens every year, and predicting the
right flu strain will continue to be a struggle, but with research, we are just
a little bit closer.
Posted by: Cynthia Bui
(1)
Do you think it is practical to rely on rational drug design techniques (designing drugs based off molecular structures) to target the M2 protein? For example, say that researchers invest years in figuring out the structural change that resulted from mutation of the M2 protein, and then develop a new compound to block the channel. Then the protein mutates again, and the new drug is rendered ineffective. In other words, do you think the payoff is worth the time and cost for these studies?
ReplyDeletePosted by Sean McDougall
I actually do not really think that relying solely on the M2 Protein is the most practical nor an effective way. As you pointed out, the it will mutate, and the new drug would become ineffective. Spending all that time, money, and research on something that can change so quickly is not worth it, and I believe and hope that scientists can find a better way to fight the flue virus.
DeletePosted by Cynthia Bui