Wednesday, February 6, 2013

Influenza Virus and its Structure

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)


  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?

    Posted by Sean McDougall

    1. 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.

      Posted by Cynthia Bui