Upon infection, Apicomplexan parasites secrete effector molecules, that modify their host cells to create a permissive environment. Rhoptries (ROP) are coccidian parasite organelles that contain mostly divergent kinase proteins (ROPK), involved into hijacking host cell signaling. The study of ROPKs in Toxoplasma gondii has identified many kinases involved in host cell signaling and immune response and demonstrated that some ROPKs are essential virulence factors. Their study in Eimeria is made difficult by the lack of efficient tools to invalidate parasite genes. Avian coccidiosis is a farm disease caused by the massive multiplication of parasites of the Eimeria genus (mainly E. tenella and E. acervulina) in the epithelial cells of the chicken's digestive tract, resulting in reduced production and high economic costs. Its control relies to a large extent on coccidiostats, which are becoming less and less effective due to the increasing development of resistance. To restore animal welfare and zootechnical performance, new treatments are needed and ROPK could be good therapeutic targets. Since data in the literature describing the role of ROPKs in Eimeria species are scarce, we studied ROPK transcription regulation all along E. tenella life-cycle. Characterization of their expression profile during infection has enabled us to identify several candidate ROPKs, which are active kinases, produced in the early parasite stage (sporozoite) and detected in the infected cell (i.e. the schizont). In the absence of an efficient knock-out system in Eimeria, it is difficult to functionally characterize the 28 members of the ROPK repertoire. We chose to overexpress the kinase of interest to access its functions. We produced a knock-in strain that overexpresses EtROP1 (ETH_00005190, ETH2_0808400) fused to YFP, under the control of the actin promoter. In parallel, we produced a control strain: a wild-type strain (Et-INRAE) that constitutively expresses m-Cherry fluorescent marker. We performed RNAseq analyses using Eimeria-infected and uninfected chicken epithelial cells. Our experimental design allowed the study of bystander-cells, i.e., non-infected cells neighbouring infected cells, to assess transcriptomic modifications resulting from soluble factors from extracellular medium. We established the host cell signature for E. tenella infection and determined the contribution of EtROP1 in host cell-signature. Taken together, EtROP1 interactome (already available) and the future phospho-proteomic analyses combined to the RNAseq should allow the identification of host cell proteins for which phosphorylation status is modified by infection and/or by EtROP1 directly, giving the first insights into the impact of secreted EtROP1 kinase on host cell signaling. As parasite ROPKs are highly divergent from eukaryotic protein kinases from hosts, ROPK may be relevant drug target candidates to control parasite infections. Our preliminary data support the essential role of EtROP1 N-terminal domain in substrate binding and catalytic activity. Although, it is unlikely that existing kinase inhibitors maybe be repurposed easily, crystallography, high-throughput inhibitor screening and in vitro phenotypic screening should facilitate the research for new anticoccidial molecules.