Aoife Heaslip

Associate Professor

Molecular and Cell Biology / Cell and Developmental Biology

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Education:  BS University College Dublin, Ph.D. University of Vermont, Post-doc University of Vermont and Indiana University, Bloomington

Research Interests: My Lab is focused on understanding the biology of human pathogen Toxoplasma gondii, an obligate intracellular protozoan parasite and the causative agent of Toxoplasmosis. Parasite survival and hence disease pathogenesis rely on its ability to secrete proteins from specialized secretory organelles, called the dense granules, into the host. We are using a combination of parasite cell biology, live cell imaging and single molecule biophysics to elucidate the molecular mechanisms underlying dense granule transport and secretion. By understanding the mechanisms underlying this essential process it is our goal to identify new targets for the development of anti-parasitic drugs.

Selected Publications:

Devarakonda PM, Sarmiento V, Heaslip AT. F-actin and myosin F control apicoplast elongation dynamics which drive apicoplast-centrosome association in Toxoplasma gondii. mBio. 2023 Sep 21:e0164023. doi: 10.1128/mbio.01640-23. Epub ahead of print. PMID: 37732764.Klassen JL. 2023. Resistance waxes for mutualists protected by wasp secretions PNAS 120(36):e2311815120 https://www.pnas.org/doi/10.1073/pnas.2311815120

Javier Periz, Jamie Whitelaw, Clare Harding, Simon Gras, Mario Igor Del Rosario Minina, Fernanda Latorre-Barragan, Leandro Lemgruber, Madita, Alice Reimer, Robert Insall, Aoife Heaslip, Markus Meissner (2017) Toxoplasma gondii F-actin forms an extensive filamentous network required for material exchange and parasite maturation.eLife 2017;10.7554/eLife.24119

Heaslip AT, Nelson SR, Warshaw DM. Dense granule trafficking in Toxoplasma gondii requires a unique class 27 myosin and actin filaments. Molecular Biology of the Cell. 2016. 27 (13): 2080-9

Heaslip AT, Nelson SR, Lombardo AT, Beck-Previs S, Armstrong J, Warshaw DM. Cytoskeletal Dependence of Insulin Granule Movement Dynamics in INS-1 Beta-Cells in Response to Glucose. PLoS One. 2014 Oct 13; 9(10): e109082

Leung JM, Tran F, Pathak RB, Poupart S, Heaslip AT, Ballif BA, Westwood NJ, Ward GE. Identification of T. gondii myosin light chain-1 as a direct target of TachypleginA-2, a small-molecule inhibitor of parasite motility and invasion. PLoS One. 2014 Jun 3;9(6):e98056. Sivagurunathan S, Heaslip A, Liu J, Hu K. Identification of functional modules of AKMT, a novel lysine methyltransferase regulating the motility of Toxoplasma gondii. Mol Biochem Parasitol. 2013 May; 189(1-2):43-53.

Armstrong JM, Krementsova E, Michalek AJ, Heaslip AT, Nelson SR, Trybus KM, Warshaw DM. Full-length myosin Va exhibits altered gating during processive movement on actin. Proc Natl Acad Sci U S A. 2012 Jan 31;109(5): E218-24.

Heaslip AT, Nishi M, Stein B, Hu K. The motility of a human parasite, Toxoplasma gondii, is regulated by a novel lysine methyltransferase. PLoS Pathog. 2011 Sep;7(9):e1002201.

Faculty of 1000 “Must Read”. Bargieri D, Menard R: “Apicomplexan parasites, including Plasmodium and Toxoplasma are eukaryotic cells that use gliding motility to locomote….” Evaluation of [Heaslip AT et al. The motility of the human parasite, Toxoplasma gondii is regulated by a novel lysine methyltransferase. PLoS Pathog. 2011 Sep; 7(9)] Faculty of 1000, 13 Oct 2011

Heaslip AT, Dzierszinski F, Stein B, Hu K. TgMORN1 is a key organizer for the basal complex of Toxoplasma gondii. PLoS Pathog. 2010 Feb 5;6(2):e1000754.

Heaslip AT, Leung JM, Carey KL, Catti F, Warshaw DM, Westwood NJ, Ballif BA, Ward GE. A small-molecule inhibitor of T. gondii motility induces the posttranslational modification of myosin light chain-1 and inhibits myosin motor activity. PLoS Pathog. 2010 Jan 15;6(1):e1000720

Heaslip AT, Ems-McClung SC, Hu K. TgICMAP1 is a novel microtubule-binding protein in Toxoplasma gondii. PLoS One. 2009 Oct 12;4(10):e7406.

de Miguel N, Lebrun M, Heaslip A, Hu K, Beckers CJ, Matrajt M, Dubremetz JF, Angel SO. Toxoplasma gondii Hsp20 is a stripe-arranged chaperone-like protein associated with the outer leaflet of the inner membrane complex. Biol Cell. 2008 Aug;100(8):479-89