Imperial College London


Faculty of Natural SciencesDepartment of Life Sciences

Visiting Researcher



+44 (0)20 7589 5111 ext 55449k.artavanis-tsakonas




606Sir Alexander Fleming BuildingSouth Kensington Campus





Host-pathogen interactions during malaria infection

Ubiquitin is implicated in virtually all aspects of cell homeostasis.  The mechanisms which control the dynamic addition and removal of ubiquitin from target proteins have been conserved throughout evolution and are important to organisms ranging from parasites to humans. The possibility of interfering with such a central mechanism in infectious pathogens presents an interesting and understudied source of new therapeutic strategies. Plasmodium parasites, the causative agents of malaria, are notorious for their ability to mutate and evade host immunity. As a result, vaccine and drug development have fallen short in reducing this disease’s debilitating morbidity and mortality.  A better understanding of the intricacies involved in host-pathogen interactions during malaria infection is necessary to uncover alternative therapeutic strategies. By using ubiquitin as a marker, our goal is to better understand the immunological changes induced in the host during infection as well as the role of ubiquitin in Plasmodium biology.

For more information please visit the lab website



Morrow ME, Kim M-I, Ronau JA, et al., 2013, Stabilization of an Unusual Salt Bridge in Ubiquitin by the Extra C-Terminal Domain of the Proteasome-Associated Deubiquitinase UCH37 as a Mechanism of Its Exo Specificity, Biochemistry, Vol:52, ISSN:0006-2960, Pages:3564-3578

White RR, Artavanis-Tsakonas K, 2012, How helminths use excretory secretory fractions to modulate dendritic cells, Virulence, Vol:3, ISSN:2150-5594, Pages:668-677

Artavanis-Tsakonas K, Kasperkovitz PV, Papa E, et al., 2011, The tetraspanin CD82 is specifically recruited to fungal and bacterial phagosomes prior to acidification., Infect Immun, Vol:79, Pages:1098-1106

White RR, Miyata S, Papa E, et al., 2011, Characterisation of the Trichinella spiralis Deubiquitinating Enzyme, TsUCH37, an Evolutionarily Conserved Proteasome Interaction Partner, Plos Neglected Tropical Diseases, Vol:5, ISSN:1935-2727

Artavanis-Tsakonas K, Weihofen WA, Antos JM, et al., 2010, Characterization and structural studies of the Plasmodium falciparum ubiquitin and Nedd8 hydrolase UCHL3., J Biol Chem, Vol:285, Pages:6857-6866

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