Characterisation of gp34, a GPI-anchored protein expressed by schizonts of Theileria parva and T. annulata

Xue, Gondga; Schubert, Conrad von; Hermann, P; Peyer, Martina; Maushagen, Regina; Schmuckli‐Maurer, Jacqueline; Bütikofer, Peter; Langsley, Gordon; Dobbelaere, Dirk

doi:10.1016/j.molbiopara.2010.03.018

Cited by 14 publications

(25 citation statements)

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“…1C12 is one of a panel of mAbs obtained after immunization of mice with T. annulata (Hissar)-infected leukocytes [34]. This mAb recognizes T. annulata schizonts, but not merozoites and piroplasms [34], [35], and serves as a useful diagnostic marker for the parasite [5], [6], [36]. The identity of this immunodominant surface antigen, however, was unknown until now.…”

Section: Resultsmentioning

confidence: 99%

“…How CLASP1 associates with the parasite surface is presently under investigation. To what extent TaSP [7] or gp34 [6] are potentially involved in these processes is presently unclear.…”

Section: Discussionmentioning

confidence: 99%

“…Proteins expressed on the surface of the schizont, or those secreted into the cytoplasm, qualify as good candidates for mediating host-parasite interactions, and yet to date only a few schizont surface proteins have been characterized in detail. gp34, a GPI-anchored schizont surface protein has been implicated in host-parasite interactions during host cell division [6]. It was proposed that TaSP, a proline-rich immunodominant T. annulata surface protein, can bind host cell α-tubulin and interact with the host cell microtubular network, but the molecular basis for these interactions is unclear [7].…”

Section: Introductionmentioning

confidence: 99%

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Recruitment of EB1, a Master Regulator of Microtubule Dynamics, to the Surface of the Theileria annulata Schizont

et al. 2013

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The apicomplexan parasite Theileria annulata transforms infected host cells, inducing uncontrolled proliferation and clonal expansion of the parasitized cell population. Shortly after sporozoite entry into the target cell, the surrounding host cell membrane is dissolved and an array of host cell microtubules (MTs) surrounds the parasite, which develops into the transforming schizont. The latter does not egress to invade and transform other cells. Instead, it remains tethered to host cell MTs and, during mitosis and cytokinesis, engages the cell's astral and central spindle MTs to secure its distribution between the two daughter cells. The molecular mechanism by which the schizont recruits and stabilizes host cell MTs is not known. MT minus ends are mostly anchored in the MT organizing center, while the plus ends explore the cellular space, switching constantly between phases of growth and shrinkage (called dynamic instability). Assuming the plus ends of growing MTs provide the first point of contact with the parasite, we focused on the complex protein machinery associated with these structures. We now report how the schizont recruits end-binding protein 1 (EB1), a central component of the MT plus end protein interaction network and key regulator of host cell MT dynamics. Using a range of in vitro experiments, we demonstrate that T. annulata p104, a polymorphic antigen expressed on the schizont surface, functions as a genuine EB1-binding protein and can recruit EB1 in the absence of any other parasite proteins. Binding strictly depends on a consensus SxIP motif located in a highly disordered C-terminal region of p104. We further show that parasite interaction with host cell EB1 is cell cycle regulated. This is the first description of a pathogen-encoded protein to interact with EB1 via a bona-fide SxIP motif. Our findings provide important new insight into the mode of interaction between Theileria and the host cell cytoskeleton.

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Section: Resultsmentioning

confidence: 99%

“…How CLASP1 associates with the parasite surface is presently under investigation. To what extent TaSP [7] or gp34 [6] are potentially involved in these processes is presently unclear.…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Recruitment of EB1, a Master Regulator of Microtubule Dynamics, to the Surface of the Theileria annulata Schizont

et al. 2013

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“…Ta‐gp34 has been previously characterised and, like CLASP1, CD2AP, and TaMISHIP, localises in a punctate pattern at the schizont surface (see Figure S9 for CD2AP and TaMISHIP structured illumination microscopy and Huber et al, , for CLASP1). Although neither the function nor the binding partner of gp34 was elucidated, a potential involvement in cytokinesis was proposed (Xue et al, ). Our data suggest that Ta‐gp34 is part of a large network of (directly or indirectly) interacting proteins at the schizont surface that mediate interactions between the schizont and the host cytoskeleton and are important for regulating cytokinesis.…”

Section: Discussionmentioning

confidence: 99%

Identification and characterisation of aTheileria annulataproline-rich microtubule and SH3 domain-interacting protein (TaMISHIP) that forms a complex with CLASP1, EB1, and CD2AP at the schizont surface

Huber

Karagenç

Ritler

et al. 2018

Cellular Microbiology

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Theileria annulata is an apicomplexan parasite that modifies the phenotype of its host cell completely, inducing uncontrolled proliferation, resistance to apoptosis, and increased invasiveness. The infected cell thus resembles a cancer cell, and changes to various host cell signalling pathways accompany transformation. Most of the molecular mechanisms leading to Theileria‐induced immortalization of leukocytes remain unknown. The parasite dissolves the surrounding host cell membrane soon after invasion and starts interacting with host proteins, ensuring its propagation by stably associating with the host cell microtubule network. By using BioID technology together with fluorescence microscopy and co‐immunoprecipitation, we identified a CLASP1/CD2AP/EB1‐containing protein complex that surrounds the schizont throughout the host cell cycle and integrates bovine adaptor proteins (CIN85, 14‐3‐3 epsilon, and ASAP1). This complex also includes the schizont membrane protein Ta‐p104 together with a novel secreted T. annulata protein (encoded by TA20980), which we term microtubule and SH3 domain‐interacting protein (TaMISHIP). TaMISHIP localises to the schizont surface and contains a functional EB1‐binding SxIP motif, as well as functional SH3 domain‐binding Px(P/A)xPR motifs that mediate its interaction with CD2AP. Upon overexpression in non‐infected bovine macrophages, TaMISHIP causes binucleation, potentially indicative of a role in cytokinesis.

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“…T. annulata recruits endbinding protein 1, a crucial component of host microtubule regulation, to its cell surface via interactions with T. annulata polymorphic piroplasm antigen, p104 [41]. The T. annulata proteins TaSE (T. annulata secretory protein) [42] and the conserved glycosylphosphatidylinositolanchored protein gp34 [43] also localize to host microtubules, although the precise roles of these proteins are not yet well understood. Recent developments in genome-scale technologies have led to the description of human metastasis-suppressor genes with potential for therapy targeting [44].…”

Section: Activation Of Invasion and Metastasismentioning

confidence: 99%

Theileria-transformed bovine leukocytes have cancer hallmarks

Tretina

Gotia

Mann

et al. 2015

Trends in Parasitology

103

122

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Characterisation of gp34, a GPI-anchored protein expressed by schizonts of Theileria parva and T. annulata

Abstract: Graphical abstractWe characterised gp34 (yellow), a GPI-anchored protein that is expressed on the surface of the schizont (red) of the transforming intracellular parasite Theileria. The host cell nucleus is stained blue.

Cited by 14 publications

References 31 publications

Recruitment of EB1, a Master Regulator of Microtubule Dynamics, to the Surface of the Theileria annulata Schizont

Recruitment of EB1, a Master Regulator of Microtubule Dynamics, to the Surface of the Theileria annulata Schizont

Identification and characterisation of aTheileria annulataproline-rich microtubule and SH3 domain-interacting protein (TaMISHIP) that forms a complex with CLASP1, EB1, and CD2AP at the schizont surface

Theileria-transformed bovine leukocytes have cancer hallmarks

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