Antibody Engineering for Pursuing a Healthier Future

Saeed, Abdullah F. U. H.; Wang, Rongzhi; Ling, Sumei; Wang, Shihua

ScFv fusion proteins are constructed by the association of heavy (V H ) and light chains (V L ) of immunoglobulins via a short peptide linker. Antigen specific scFv can be easily generated by phage display. These fusion proteins have extensive applications in cancer therapeutics such as in lymphatic invasion vessels, colon cancer, hepatocarcinoma, and diagnostics of human disease (Tonelli et al., 2012) . Moreover, scFv have been widely used with phage display panning i.e., an affinity selection technique, to construct ligands to detect toxins produced by various pathogenic entities in vitro or in vivo. Similarly, coexpression vector systems have been used to prevent and cure diseases by scFv. Currently, various scFv fragments have been constructed against toxins and virulence factors of pathogens (Tonelli et al., 2012; Wang et al., 2013 Wang et al., , 2016 . Additionally, a method for rapid and effective high-affinity GFP-based antibody production corresponding to scFv was developed. It was demonstrated by inserting CDR3 into green fluorescence protein (GFP) loops for improved disease diagnosis and therapy (Wang et al., 2014b) . Skp co-expressing scFv has high solubility and binding activity to antigen thermolabile hemolysin (TLH) (a pathogenic factor of Vibrio parahaemolyticus) and was developed by using pACYC-Duet-skp co-expression vector. This scFv was constructed to detect TLH directly in real samples. Furthermore, an antibody was developed against TLH that showed strong neutralizing effects on TLH-induced cell toxicity (Wang et al., , 2007 (Wang et al., , 2014a Chen et al., 2015) .