Theileria highjacks JNK2 into a complex with the macroschizont GPI ‐anchored surface protein p104

AbstractConstitutive JNK activity characterizes bovine T and B cells infected withTheileria parva, and B cells and macrophages infected withT. annulata. Here, we show thatT. annulata infection of macrophages manipulates JNK activation by recruiting JNK2 and not JNK1 to the parasite surface, whereas JNK1 is found predominantly in the host cell nucleus. At the parasite's surface JNK2 forms a complex with p104 a GPI ‐anchoredT. annulata plasma membrane protein. Sequestration of JNK2 depended on PKA ‐mediated phosphorylation of a JNK‐binding motif common toT. parva and a cell penetrating peptide harbouring the conserved p104 JNK ‐binding motif competitively ablated binding, whereupon liberated JNK2 became ubiquitinated and degraded. Cytosolic sequestration of JNK2 suppressed small mitochondrial ARF‐mediated autophagy, whereas it sustained nuclear JNK1 levels, c‐Jun phosphorylation and matrigel traversal. Therefore,T. annulata sequestration of JNK2 contributes to both survival and dissemination ofTheileria‐transformed macrophages.

Source: Cellular Microbiology - November 9, 2018 Category: Microbiology Authors: Perle Latr é De Laté, Malak Haidar, Hifzur Ansari, Shahin Tajeri, Eszter Szarka, Anita Alexa, Kerry Woods, Attila Reményi, Arnab Pain, Gordon Langsley Tags: RESEARCH ARTICLE Source Type: research