A Desperate Response to the West African Ebola Outbrake

     The Ebola virus disease (EVD) first appeared in 1976 but it has reappeared several time over the course of the last four decades. The virus, which was originally introduced into the human population through zoonoses, later mutated into a blood born pathogen that could be transmitted through human bodily fluids. Since its inception into the human population there have been three major outbreaks of the Ebola virus in human history. The largest and most recent one appeared in 2014 in West Africa and since then has spread to countries such as: Italy, Mali, Nigeria, Senegal, Spain, the United Kingdom, and the United States. The mutation of the EVD has resulted in a severe outbreak across borders and because of this it has quickly attracted the attention of the institutes like the World Health Organization. Containing the spread of the virus has become the leading concern among health officials and has prompted the production of new antiviral drugs. According to TheScientist.com there are four drugs being studied, an antiviral and three monoclonal antibodies, which are being developed by DRC’s National Institute of Biomedical Research and the US National Institutes of Health. The experimental therapies will include the antiviral drug Remdesivir and three monoclonal antibodies: ZMapp, REGN and mAb 114. These four drugs will be used in clinical trials to see whether or not they will improve patient's chances of survival in the midst of this outbreak. Unlike most trials, this study is a little unorthodox in terms of controlled environments. The study has unique challenges such as monitoring the drugs in environments that contain violence, kidnappings and conflicts. The situation was put into perspective when STATnews quoted a WHO representative saying "I don’t think the world quite appreciates the challenge of the environment in which this is happening... People are being shot at, and it’s not just the occasional bit of gunfire" (Farrar, 2018). The environment in which these studies are being done is anything but auspicious but the situation is dire and health officials are desperate. Researchers and health officials expect to see results soon but in the meantime they will continue to monitor the progress of these experimental drugs in the hope of seeing a positive results.

How Honey Bees Fight Infections

Bees in their hive

Honey bees, bees in general, play a big role in our daily lives- both directly and indirectly. They provide us honey and help pollinate our crops we use as food or feed for our livestock. However, these creatures are also vulnerable to viruses like any other organism. Like many organisms, they have learned to fight against some of these viruses.

According to an article in Science Daily, honey bees use a variation of genes to protect themselves against viruses. Each year, beekeepers lose approximately a third of their bees due to viral infections. Currently, there are no ways of preventing these infections but scientists have found that RNAi pathways can help combat these viruses. Researchers and beekeepers hope to synthesize RNAi because it effectively destroys viral RNA. If they are successful, they can help to save a large portion of bees lost every year.

This article helps to put things into perspective; while we look in fear at anti-biotic resistant viruses are creeping their ways into our hospitals, we forget that this is also happening to other organisms. It points out that as we create super bugs- viruses are changing in nature, independent of our anti-biotics and affecting other organisms. If the artificial RNAi is created for these viruses, what's stopping the viruses from evolving further?
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Flu virus key machine: First complete view of structure revealed

Link to the Article

Scientists at EMBL Grenoble have recently obtained a complete view of one of the flu virus' key machines, influenza virus polymerase. This allows scientists to finally understand how the machine works and could lead to new drugs being designed to stop influenza. The influenza virus polymerase copies the virus' genetic material to package into new viruses, and it reads out the instructions in that genetic material to make viral mRNA. The structures revealed shows how the polymerase recognizes and binds to viral RNA and not just any available RNA. They also show that the three component proteins of the polymerase are intertwined.

Using X-ray crystallography, scientists were able to determine the atomic structure of the polymerase for both Influenza A and B. The scientists found that the one key difference in the polymerase of both structures, in one structure a part of the polymerase can swivel around to a large degree. This explains exactly how the polymerase can use host cell RNA to kick-start the production of viral proteins. With this knowledge, researches hoping to stop influenza now have a much wider range of potential targets at their disposal.

Obtaining the complete view of the influenza polymerase now provides scientists with more information and areas where they can attack the structure. They can view what is doing what and how it is accomplishing it, then they can design a drug that stops that mechanism. This could lead to a new drug that is designed to stopping Influenza A and preventing any future pandemics caused by the virus.