Research
As a class of pathogens parasites tend to establish chronic infections. This means that they have adapted intricate mechanisms of avoiding host immune responses, limiting tissue damage, and modulating their immediate surrounding to support their presence. By understanding how they adapt themselves to their environment, we stand to learn important information about host tissues they colonize. We have a particular interest in how parasites interfere with and manipulate the host ubiquitin-proteasome system.
We currently focus on two organisms: the malaria parasite, Plasmodium falciparum, and the nematode Trichinella spiralis.
Publications
White RR, Ponsford AH, Weekes MP, Rodrigues RB, Ascher DB, Mol M, Selkirk ME, Gygi SP, Sanderson CM, Artavanis-Tsakonas K. Ubiquitin-Dependent Modification of Skeletal Muscle by the Parasitic Nematode, Trichinella spiralis. PLoS Pathog. 2016 Nov 21;12(11):e1005977.
Morrow ME, Kim M, Ronau JA, Sheedlo MJ, White RR, Chaney J, Paul LN, Lill M, Artavanis-Tsakonas K, Das C. Structural analysis of ubiquitin recognition by the proteasome-associated deubiquitinase UCH37 from Trichinella spiralis. Biochemistry. 2013, 52 (20): 3564-3578.
White RR, Miyata S, Papa E, Spooner E, Selkirk ME, Gounaris K, Artavanis-Tsakonas K. Characterisation of the Trichinella spiralis Deubiquitinating Enzyme,TsUCH37, an Evolutionarily Conserved Proteasome Interaction Partner. PLoS NTD. 2011, Oct 4(10):e1340.
Artavanis-Tsakonas K,Weihofen WA,Antos JM, Coleman BI, Comeaux CA, Duraisingh MT, Gaudet R, Ploegh HL. Structural studies and characterization of the Plasmodium falciparum ubiquitin and Nedd8 hydrolase UCHL3. J Biol Chem. 2010, Feb 26;285(9):6857-66.
Frickel EM, QuesadaV, Muething L, Gubbels MJ, Spooner E, Ploegh H, Artavanis-Tsakonas K. Apicomplexan UCH- L3 retains dual specificity for ubiquitin and Nedd8 throughout evolution. Cell Microbiol. 2007, 9(6):1601-10.
