Therapeutic monoclonal antibodies (mAbs) have evolved into an important class of effective medicine in treatment of various diseases. Since the antibody molecule consists of two identical heavy chains (HC) and two light chains (LC)， each chain encoded by two different genes， their expressions at similar levels are critical for efficient assembly of functional recombinant mAbs. Although the plant-based expression system has been tested to produce fully assembled recombinant mAbs， coordinately expressing HC and LC at similar levels in a transgenic plant remains a challenge. A sequence coding for a foot-and-mouth disease virus (FMDV) 2A peptide has been successfully used to link two or more genes， which enable the translated polyprotein to be "self-cleaved" into individual protein in various genetically modified organisms. In the present study， we exploited the usage of F2A in Ebola virus monoclonal antibody (EBOV mAb) production. We found that transgenic tobacco plants carrying a transcription unit containing and linked by not only produced similar levels of HC and LC but also rendered a higher yield of fully assembled EBOV mAb compared to those expressing and in two independent transcription units. Purified EBOV mAb bound to an Ebola epitope peptide with apparent -values of 90.13-149.2 nM， indicating its proper assembly and high affinity binding to Ebola epitope peptide. To our knowledge， this is the first report showing mAb production by overexpressing a single transcription unit consisting of ， and 2A in stable transformed tobacco plants.