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Scientists take a high resolution look at the life cycle of Ebola virus

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Posted June 29, 2015

Team of scientists from The Scripps Research Institute have achieved a high resolution look at the key part of life cycle of Ebola virus. This research shows how Ebola virus assembles and provides space for new approaches on how this often-fatal infection could be stopped. It provides hope that soon there will be new effective antiviral therapeutics developed.

Scientists used a technique called x-ray crystallography to obtain a high-resolution image of life cycle of Ebola virus. It revealed how VP35 protein helps protect Ebola virus from the body’s immune system. Image courtesy of scripps.edu.

Scientists used a technique called x-ray crystallography to obtain a high-resolution image of life cycle of Ebola virus. It revealed how VP35 protein helps protect Ebola virus from the body’s immune system. Image courtesy of scripps.edu.

New high resolution look at life cycle of Ebola virus demonstrates how a viral protein called VP35 protects Ebola virus as well as related Marburg virus from the immune system of the body. VP35 helps the viral protein to coil and form a protein shell, called nucleocapsid, around the virus’s genetic material. This effectively blocks Ebola’s (or Marburg’s) genetic material from the view of immune system and makes it impossible for the organism to mount an effective defence. Even though this research is based on information that was obtained on previous work in lab of Professor Erica Ollmann Saphire, up until now scientists were not able to get a better look at coiling process.

To observe the coiling process in great detailed scientists have used an imaging technique called x-ray crystallography. Professor Erica Ollmann Saphire, who was senior author of the new study too, said that “this higher resolution is critical for design of much-needed antiviral therapeutics,” and “these structures provide the blueprints that we need to see key vulnerabilities to attack”. Using x-ray crystallography scientists were able to show exactly how VP35 helps the viral protein that creates the nucleocapsid around the virus’s genetic material.

The new study also demonstrates how the VP35 protein prevents the nucleocapsid from assembling incorrectly. In fact, the resolution, at which scientists observed the life cycle of Ebola virus, is so high that they could even see key atoms and structures called side chains—crucial pieces for moving forward with structure-based drug design. However, results of the research could be useful in developing innovative therapeutics to other viruses as well, not just Ebola virus. Scientists say that this structure that they revealed is most likely common for other filoviruses as well, such as Marburg, Sudan, Bundibugyo and Reston viruses. Furthermore, the new knowledge from the study could be applied to Mononegavirales too – it is an order of viruses that includes measles and rabies.

Ebola virus first appeared in 1976. However, the largest and most complex Ebola outbreak occurred in 2014 in West Africa. There have been outbreaks before, but in this one there have been more cases and deaths in this outbreak than all others combined. Because Ebola is extremely contagious, spreading through direct contact, with the blood, secretions, organs or other bodily fluids of infected people, and with surfaces and materials contaminated with these fluids.

The outbreak of Ebola virus attracted a lot of media attention and is still not fully controlled in the region, spreading fear and asking for quick solutions to prevent such outbreaks in the future. New drug treatments are needed as well, since the disease often has fatal results. That is why researches like this are extremely useful, even if only proved a better look of how virus develops, because to create new innovative treatments scientists need to know how Ebola and related viruses trick the immune system.

Sources: scripps.edu, WHO

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