The Higgins laboratory study the molecular basis for host-parasite interactions in malaria and sleeping sickness. They investigate the mechanisms of erythrocyte invasion by the malaria parasite, and study how adhesive proteins sent to the surface of the infected erythrocyte cause endothelial adhesion and severe malaria. They also determine how trypanosomes are able to resist human innate immune factors and cause human infection. They also use this information to design novel and improved vaccine immunogens.
Hsieh, F., Turner, L., Bolla, J.L., Robinson, C.V., Lavstsen, T. and Higgins, M.K. (2016) The structural basis for CD36 binding by the malaria parasite. Nature Comm 7 12837
Lane-Serff, H., MacGregor, P., Peacock, L., Macleod, O.J., Kay, C., Gibson, W., Higgins, M.K. * and Carrington, M. * (2016) Evolutionary diversification of the trypanosome haptoglobin-haemoglobin receptor from an ancestral haemoglobin receptor. eLife e13044
Lau, C.K.Y, Turner, L., Jespersen, J.S., Lowe, E.D., Petersen, B., Wang, C.W., Petersen, J.E.V., Lusingu, J., Theander, T.G., Lavstsen, T. and Higgins, M.K. (2015) Structural conservation despite huge sequence diversity allows EPCR binding by the PfEMP1 family implicated in severe childhood malaria. Cell Host and Microbe 17 118-129
Lane-Serff, H., McGregor, P., Lowe, E.D., Carrington, M. and Higgins, M.K. (2014) Structural basis for ligand and innate immunity factor uptake by the trypanosome haptoglobin-haemoglobin receptor. eLife 3 e05553
Wright K.E., Hjerrild K.A., Bartlett J., Douglas A.D., Jin J., Brown R.E., Illingworth J.J., Ashfield R., Clemmensen S.B., de Jongh W.A., Draper S.J. and Higgins M.K. (2014) Structure of malaria invasion protein RH5 with erythrocyte basigin and blocking antibodies. Nature 515 427-30
Turner L., Lavstsen T., Berger S.S., Wang C.W., Petersen J.E.V., Avril M., Brazier A.J., Freeth J., Jespersen J.S., Nielsen M.A., Magistrado P., Lusingu J., Smith J.D., Higgins M.K., Theander T.G. (2013) Severe malaria is associated with parasite binding to endothelial protein C receptor. Nature 498 502-5.