###### Abstract
It is assumed that hyphal mechanical pressure combined with enzymatic hydrolysis is responsible for the invasion process in which _S. mycopparasitica_ parasitizes the host. These assumptions related to several mycopparasitism-related genes and transcripts have not yet been investigated in _S. mycopparasitica_, which led to our attention. Previous studies in our group have demonstrated that _S. mycopparasitica_ parasitizes different _Fusarium_ species through diphasic interactions, while its adaptability to the _Fusarium_ hosts has been demonstrated using in vitro compatibility assays [2]. Moreover, the biodegradation or biotransformation ability of _S. mycopparasitica_ to mycotoxins such as zearalenone, deoxynivalenol, and its derivatives (3-acetyl-deoxynivalenol and 15-acetyl-deoxynivalenol) has been uncovered by means of biodegradation experiments [9]. In general, mycopparasites produce cell wall degrading enzymes (CWDEs) such as glucanases and chitinases involved in the destruction of the phytopathogenic host cell wall [10,11]. The genes encoding CWDEs are often highly upregulated during the early stages of mycopparasitism [12,13]. Genes encoding the components of a mitogen-activated protein kinase (MAPK) [14,15], NADPH oxidase, oxalate decarboxylase, transcription factors [16,17], and the peroxisome and heat shock [18,19] are vital regulatory factors in mycopparasitism. In other instances, expression of mycopparasitism- and secondary metabolism-related genes are often differentially regulated in the presence or absence of a phytopathogenic host [20] which unveils the importance of in vivo interaction studies to discover different regulation pathways in mycopparasites. When the mycopparasite interacts with a host in a particular environment, the cell wall (rigid and stable structure, also a storage site of regulatory molecules that sense the presence of pathogenic microbes) and the cell membrane (more flexible and responding to the dynamic changes) are the first barriers to recognize abiotic and biotic factors. The cell membrane commonly including membrane-bound or integrated proteins is expected to play a crucial role associated with mycopparasitism. A recent finding by [PERSON] and [PERSON] (2021) supported this insight. Five different lifestyle-specific genes, representing endophytism, entomopathogenism, plantpathogenism, mycopparasitism, and symbiosis [21], all encoded abundant proteins with multiple functional signatures. The genes were implicated in transmembrane transport and oxidation/reduction processes as integral components of membranes in fungi across their lifestyles and evolutionary functions. In the well-known biocontrol agent _Trichoderma_, which is an extensively studied general mycopparasite, different ABC transporter genes have been reported to be upregulated during the tripartite mycopparasite-fungal pathogen-plant system [22]. Indeed, ABC transporter genes are involved in several _Trichoderma_'s mycopparasite activities by sustaining an efficient biocontrol. The pleiotropic drug resistance (PDR) family of ABC transporterssuch as the _Taabc2_ gene in _Trichoderma atroviride_, regulates fungal antagonism and the colonization process on phytopathogens under fluctuating environmental conditions [23]. Another PDR family of genes within the ABC-G subfamily members, including _Pdr5p_ in the model yeast _Saccharomyces cerevisiae_, has been described as active efflux pumps conferring resistance to structurally and functionally unrelated drugs and xenobiotics: antibiotics, fungicides, detergents, ionophores, steroid hormones, and anticancer drugs [24; 25; 26]. In mycoparsaite _Clonostachys rosea_, _abcG5_, belonging to the PDR family, seems to be an essential ABC transporter gene responsible for antagonistic and biocontrol activity [27]. Interestingly, _abcG5_ gene expression was induced by mycotoxin zeanelenone [28], while its deletion in _C. rosea_ resulted in lowering fungal tolerance to zeanelenone produced by plant pathogenic _Fusarium_ species [27]. Recent research on _C.