Summary: The frog species Hydrophylax bhuvistaraa secretes slime that contains a peptide that targets human H1 flu virus. Urumin, the peptide targets viruses without being toxic and harmful to human cells. This could present new ways to fight influenza in humans. Urumin targets hemagglutinin, completely denaturing the virus after exposure.
Connections: We learned about the antibiotic penicillin in class. Penicillin is made by a fungi in order to kill bacteria it might be in competition with for nutrients. Urumin, which is secreted by the frogs, is also for the frogs own benefit. Just in the way that we sued penicillin, a naturally produced antibiotic to our advantage, we hope to use Urumin to treat influenza.
Critical Analysis: This article seems very scientifically accurate. However, I do think mainstream media tends to sensationalize these kinds of discoveries. They had quotes from experts backing up their claims, but it would likely be a long time before Urumin would ever be able to actually be used in humans.
Question: What exactly is hemagglutinin in the H1 virus, what makes it unique to the virus?
4 Comments for “Researchers use frog mucus to fight the flu”
This article sounds very interesting!! and i like how you connected penecillin produced by fungi to Urumin produced by the frog that will protect itself. I hope this gets further researched and soon and be readily available 😀
I agree with you, I thought the article was well written and scientifically accurate. I also agree with your statement about how media treats these kinds of discoveries, I think they tend to make a lot more fuzz about it then there is, and that they make it seem like this is something that is happening as we speak, but there is so much time between this research and the trials of the final product is done.
From the little research that I did, I found out that hemagglutinin is a glycoprotein found on the surface of influenza viruses. It is responsible for binding the virus to cells with sialic acid on the membranes, such as cells in the upper respiratory tract or erythrocytes. Hemagglutinin has 18 antigens and HA1 is one of them.
Amanda Jean Garnersays:
I think you’re right that mainstream media tends to hyperbolize these scientific discoveries, but this article does point out that much more research is needed to determine how efficient this peptide could be in helping humans fight off the H1N1 virus, since it’s only been proven effective in mice and underneath a microscope. However, this was only one line in the article and I do think it emphasized how excited scientists are about this new finding.
The CDC has some useful information as for what hemagglutinin (HA) is. It’s one of two types of proteins found on the cell surface of Influenza A viruses (the other being neuraminidase, abbreviated NA). There are 18 types of hemagglutinin proteins and 11 neuraminidase subtypes, so H1N1 refers to those viral surface proteins. Being specific kind of protein on its surface, I think this explains (or at least partially explains) why the peptide these frogs secrete is only effective with H1 and not H3, for example, but hopefully someday soon they can explain the mechanism behind this.
I thought the article was very interesting! I do slightly disagree in the analogy to penicillin, though. Penicillin kills the ability of bacteria to form cell walls. This chemical kills proteins found on viruses, so there’s a bit of a difference to me. I think this is interesting because it connects to class where we talked about how people who got chicken pox were immune to smallpox later in life. This is because the chicken pox and the smallpox are anatomically similar, so your body already had antigens to it. In the same way the frog had antigens to H1 virus because it was exposed to an amphibian virus that is anatomically similar. Fascinating. To answer your question, hemagglutinin is a protein expressed on virus’ surface which is able to bind to receptors in human respiratory tracts. What makes hemagglutinin unique to the virus is its shape, formed by the amino acids that comprise it. This specificity allows it to lock in to the target cells so well due to physical shape as well as polar and non-polar bonds with the target cell.