Measles is an important disease worldwide that is highly infectious, causing the deaths of over 100000 people annually. We used advanced electron microscopy and image processing methods to make a a three-dimensional model of measles virus. The new model helps to explain many previous, unaccounted for observations in the life cycle of the virus. Measles virus belongs to a family of viruses whose members are all pleomorphic enveloped viruses. All the members of this family contain a so called “matrix” protein which has previously been thought to line the inside of the envelope and play a major role in the budding of the virus from the cell. We show that matrix actually forms helical tubes inside the virus that are wrapped around the viral genome and nucleocapsid. So matrix helps to compact the genome to fit it into the virus. Thus matrix can regulate both the start of virus replication in the cell, and also the movement of the genome within the cell. The understanding of virus structure at the molecular level can help in the design and development of new antiviral drugs. The measles virus research was carried out as a collaboration with researchers from Oxford and Turku Universities. Read more in the original article in PNAS Liljeroos, L., Huiskonen, J., Ora, A., Susi, P. & Butcher, S.J. (2011) Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions. or in the news stories such as this from Tiede: http://www.tiede.fi/uutiset/4472/tuhkarokkovirus_kayttaa_kierretta from Medical News Today http://www.medilexicon.com/medicalnews.php?newsid=236536 and Chemical and Engineering News http://www.cen-online.org/articles/89/i44/Microscopy-Reveals-New-Layout-Measles.html

Low-density lipoprotein (LDL) particles are the major carriers of cholesterol in the human circulation. They have key roles in both cholesterol physiology and in the development of atherosclerosis. Together with researchers from the Wihuri Research Institute, Aalto University and Oulu University we characterised the structure of LDL particles at the human body temperature to understand the organisation of the lipids and protein that they are made from.See the article for more details Kumar, V., Butcher, S.J., Öörni, K., Engelhardt, P., Heikkonen, J., Kaski, K., Ala-Korpela, M., Kovanen, P.T. (2011) Three-dimensional cryoEM reconstruction of native LDL particles to 16Å resolution at physiological body temperature. PLoS ONE 6(5): e18841. doi:10.1371/journal.pone.0018841.

Human parechovirus is just one of the many causes of childhood infections. By examining the structure of the virus in complex with a protein from human cells, we can understand more about the first stages of the infection. In order to start an infection, the virus has to get into a host cell. It does this by attaching to human proteins on the outside of the cell, in this case big molecules called integrins. The integrins then drag the virus into the cell where it can start to replicate. See the article for more details Seitsonen, J., Susi, P., Heikkilä, O., Sinkovits, R.S., Laurinmäki, P., Hyypiä, T., Butcher, S.J. (2010). Interaction of αVβ3 and αVβ6 integrins with Human parechovirus 1. J. Virol 84:8509 - 8519

Hantaviruses are borne by rodents such as voles. They are spread in the droppings of the animal, and can infect humans who come into contact with the droppings, especially farm workers and gardeners. Some hantaviruses can cause severe haemorraghic fever which can lead to death. We studied a non-pathogenic hantavirus called Tula virus, as a useful model to understand hantavirus structure and assembly. We discovered the organisation of the major proteins that interact with the host during entry, and this could help to drive development of drugs to prevent, or relieve hantavirus infection. See the article: Huiskonen, J.T., Hepojoki, J., Laurinmäki, P., Vaheri, A., Lankinen. H., Butcher, S.J., Grunewald, K. (2010) Electron cryo-tomography of tula hantavirus suggests a unique assembly paradigm for enveloped viruses. J. Virol. 84:4889 - 4897