{"id":11950,"date":"2017-12-20T14:41:07","date_gmt":"2017-12-20T13:41:07","guid":{"rendered":"https:\/\/news.embl.de\/?p=11950"},"modified":"2024-03-22T11:51:03","modified_gmt":"2024-03-22T10:51:03","slug":"futures-unravelling-influenza","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/futures-unravelling-influenza\/","title":{"rendered":"Futures: Unravelling influenza"},"content":{"rendered":"\n
\"A<\/a>
EMBL group leader Stephen Cusack. PHOTO: EMBL<\/figcaption><\/figure><\/div>\n\n\n\n

Many of us have experienced influenza \u2013 or \u2018flu\u2019 \u2013 as an illness with unpleasant symptoms like fever, coughing and sneezing, and an aching body, but usually we recover within a couple of weeks. However, certain strains of flu can be much more harmful \u2013 particularly in vulnerable groups like children, the elderly, and pregnant women \u2013 and around the world there are still many hundreds of thousands of flu-related deaths each year.<\/p>\n\n\n\n

One way of tackling this problem is by developing anti-influenza drugs. A promising target for these drugs is one of the flu virus\u2019s enzymes, influenza polymerase. My research group determined the molecular structure of this enzyme in 2014. It\u2019s an assembly of three proteins that makes copies of the flu virus\u2019s genetic material and also transcribes it \u2013 in other words, uses it to create strands of messenger RNA (mRNA), which tells a virus-infected cell to make viral proteins. To be recognized by the cell\u2019s protein-making machinery, all mRNAs have to have a special chemical structure at the beginning known as the cap. The flu virus can\u2019t make the cap itself, so instead it steals it from host cell mRNA.<\/p>\n\n\n\n

We\u2019ve been able to show how this works in three dimensions. The influenza polymerase enters the nucleus of an infected cell and binds to the human form of the polymerase enzyme, which makes human mRNA. It binds to the cap of a newly formed human mRNA strand and cuts out a short piece called a primer that contains the cap structure. The primer is then flipped into the active site of the viral polymerase to kick-start synthesis of viral mRNA. It\u2019s an ingenious strategy known as \u2018cap-snatching\u2019, which is unique to the flu virus.<\/p>\n\n\n\n

Capturing structures<\/h2>\n\n\n\n

We\u2019d like to know in more detail how influenza polymerase works. In the past we\u2019ve mainly used X-ray crystallography to figure out protein structures, but you first need crystals of the protein you want to study, which can be difficult or in some cases impossible to obtain. It took several years before we succeeded in doing this with influenza polymerase. More recently, we\u2019ve been able to make use of cryo-electron microscopy (cryo-EM), which involves rapidly freezing samples at very low temperature and imaging them using a beam of electrons, allowing us to observe detail at much smaller scales than is possible using a conventional light microscope. Since cryo-EM doesn\u2019t require samples to be highly ordered \u2013 as in a crystal \u2013 we\u2019re able to see individual influenza polymerase molecules in many different shape configurations in the same sample, allowing us to piece together the whole sequence of changes that the enzyme undergoes during its normal activity.<\/p>\n\n\n\n

The structure of influenza polymerase is hard to determine using cryo-EM because it\u2019s a small protein complex with flexible, moving parts. However, we\u2019ve recently used cryo-EM to determine a detailed structure of it, comparable in quality to those obtained using X-ray crystallography. We\u2019ve benefited from recent amazing developments in cryo-EM that have revolutionised the technique \u2013 the pioneers of these developments, including EMBL alumnus Jacques Dubochet<\/a>, were awarded the Nobel Prize in Chemistry this year. Our continued cryo-EM studies on influenza polymerase will also benefit from the newly opened cryo-EM facility<\/a> on the European Photon and Neutron science campus \u2013 where EMBL Grenoble is located.<\/p>\n\n\n\n

Finding targets<\/h2>\n\n\n\n

Understanding the structure of influenza polymerase makes it easier to identify drug candidates that could stop it from working, halting the progress of the virus by preventing new viruses from being made. The parts of the influenza polymerase involved in cap-snatching, for instance, are prime targets for antiviral drugs. Many researchers and pharmaceutical companies are currently working on this problem, and I\u2019m confident that in five years we\u2019ll have potent anti-influenza drugs that target influenza polymerase.<\/p>\n\n\n\n

We\u2019ll also understand more about how the polymerase functions in the physiological environment of the cell. For example, how does it manage to sneak in and steal caps from strands of human mRNA, when these caps are usually protected by specialised proteins? To answer this and other questions, we\u2019ll need not only the cryo-EM technique described above, but also cryo-electron tomography \u2013 an extension of cryo-EM that should make it possible to obtain three-dimensional images of influenza polymerase at work inside the nucleus of a host cell. These studies will bring many benefits, such as an improved understanding of the species barrier that usually prevents humans from being infected by strains of flu that infect other animals, such as birds. Occasionally this species barrier can be crossed \u2013 often with severe consequences. Understanding how that happens will be an important step toward preventing flu outbreaks and reducing the widespread health problems they cause.<\/p>\n\n\n

\n

<\/p>\n

The European Research Council (ERC) is a European funding body that offers substantial five-year grants to support researchers at all stages of their careers. Inspired by the ERC’s tenth anniversary in 2017, we asked some of EMBL’s ERC grantees to look ahead another ten years and share their vision for their field of research.<\/p>\n

Find out more about EMBL’s ERC grantees<\/a>.<\/p>\n

More articles in EMBL’s Futures series<\/a>.<\/p>\n

<\/p><\/div>\n","protected":false},"excerpt":{"rendered":"

ERC grantee Stephen Cusack shares his vision for the next ten years<\/p>\n","protected":false},"author":45,"featured_media":11965,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[29,335,312,136,266,495,37,32,70,35],"embl_taxonomy":[],"class_list":["post-11950","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-crystallography","tag-cusack","tag-drug-discovery","tag-electron-microscopy","tag-enzyme","tag-future","tag-grenoble","tag-health","tag-rna","tag-structural-biology"],"acf":{"article_intro":"

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