Monday, September 26, 2016

New 'Trojan Horse' Antibody Strategy Shows Promise Against All Ebola Viruses

Ebola is a virus that the general public tends to freak out about as soon as a case pops up. A lot of this stems from not being educated on the topic but a lot of it also comes from there not being a highly effective or approved vaccine yet. Ebola has killed thousands in Africa so far in about two dozen different outbreaks. Researchers at Albert Einstein College of Medicine have found a strategy to target an Achilles' heel that all known viruses of Ebola have. So far, two antibodies have been able to stop the invasion of Ebola into human cells. Up until this research, the most promising antibodies were monoclonal antibodies but these only neutralize a specific virus. Ebola virus Zaire has monoclonal antibodies that can neutralize the virus but Sudan and Bundibugyo do not have any antibodies known to neutralize them yet. The goal is to find a monoclonal antibody that protects against all five ebolaviruses. In 2011, a group of researchers were able to expose the Achilles' heel of all of the ebolaviruses. They must all bind to a specific host-cell protein to infect and multiply. This also holds true to the Marburg virus. They realized that if the specific protein was neutralized or if the viral protein that binds was neutralized, Ebola would not be able to multiply. However, these targets lay deep in cells so that the immune system does not see them and antibodies cannot protect them. This is where the "Trojan horse" strategy comes into play. This strategy tricks the virus into carrying the antibody with them into the host cell which would neutralize the virus before it is able to bind and multiply. So far, when tested in the lab when harmless viruses are genetically altered to have all of the glycoproteins from all five ebolaviruses, all five viruses were neutralized. Next, mice were injected with the two most lethal ebolaviruses. The mice did not live due to the fact that the antibodies were specifically designed to bind to the human protein. The researchers plan to test the antibodies on nonhuman primates next. This research could be a huge breakthrough with many viruses. If researchers can continue to find the Achilles' heel for more and more viruses, antibodies could be made more diverse since there is a better understanding. This could protect people from many viruses as a whole.

See more at: http://www.einstein.yu.edu/news/releases/1196/new-trojan-horse-antibody-strategy-shows-promise-against-all-ebola-viruses/#sthash.eZ4rfMru.dpuf

Wednesday, September 21, 2016

Extremotolerant tardigrade genome and improved radiotolerance of human cultured cells by tardigrade-unique protein

Tardigrades or water bears are extremely small aquatic animals that can tolerate extreme dehydration and once dehydrated can tolerate a variety of extremes. The most tolerant species is Ramazzottius varieornatus. This species has lost the gene pathways that promote stress and have a high expression of species unique proteins. Tardigrade unique proteins were used to test X-ray induced DNA damage on cultured human cells and the damage was suppressed by 40%. These unique proteins are the start of understanding how tardigrades are able to withstand so many physical stressors and environments once they become dehydrated. This can enable the study of new genes and mechanisms that can be used to stand high stress and be used for protection.

More can be read about this at: http://www.nature.com/ncomms/2016/160920/ncomms12808/full/ncomms12808.html

Wednesday, September 14, 2016

Snail venom holds key to better diabetes treatments

Diebetes is a huge problem millions of Americans deal with on a daily basis but what if human insulins were not the best insulins? Researchers in Australia and the U.S. have teamed up and studies have shown that the insulin found in the venom of cone snails can bind to human insulin receptors. Human insulins have to be be structurally altered before they are able to function correctly where the snail insulin is already structurally correct and can immediately bind to the receptors. Without the structural change happening, the snail insulin can bind and speed up the cell signaling process. The researchers are now trying to use this information to design new treatments. I personally do not have to ever deal with diabetes but I know many people that do. Research like this can definitely help many people get the immediate shot of insulin they need and it can start helping faster and more effectively. Hopefully this will be able to be a long term fix and will be something that is not too cost effective or hard to come by.

To read more information: http://www.wehi.edu.au/news/snail-venom-holds-key-better-diabetes-treatments

Tuesday, September 6, 2016

Molecular Biology Post 1

Lately in the news we have heard about the flesh-eating bacteria of group A streptococcus. Due to many studies at the Houston Methodist Research Institute and the U.S. National Institute of Allergy and Infectious Diseases, the mechanism of the bacterial disease has been identified based off of sequencing of almost 5,000 group A streptococcus genomes. The severity of the cases caused by group A streptococcus vary in severity. The most common case is strep throat but can be as sever as necrotizing fasciitis. Once sequencing the genome, the original hypothesis was failed to be rejected, changes in the genetic makeup have caused new epidemics. The alterations were in genes that encode two dominant toxins. The genetic changes result in production of single nucleotide polymorphisims, two of which highly increased the production of two toxins that are harmful to humans. 

I believe that this method could pave the road for many other discoveries when it comes to unknown mechanisms. This bacteria just so happened to be a very good model organism so sequencing was easier than a bacteria with a massive genome or one that lacks scientists' knowledge. By sequencing, the cause of many diseases was able to be pinpointed down to the exact genes that were being altered. 

This article was found at https://www.sciencedaily.com/releases/2015/08/150810172453.htm