title: Progress in the development of immunoanalytical methods incorporating recombinant antibodies to small molecular weight biotoxins.
abstract: Rapid immunoanalytical screening of food and environmental samples for small molecular weight (hapten) biotoxin contaminations requires the production of antibody reagents that possess the requisite sensitivity and specificity. To date animal-derived polyclonal (pAb) and monoclonal (mAb) antibodies have provided the binding element of the majority of these assays but recombinant antibodies (rAb) isolated from in vitro combinatorial phage display libraries are an exciting alternative due to (1) circumventing the need for experimental animals, (2) speed of production in commonly used in vitro expression systems and (3) subsequent molecular enhancement of binder performance. Short chain variable fragments (scFv) have been the most commonly employed rAb reagents for hapten biotoxin detection over the last two decades but antibody binding fragments (Fab) and single domain antibodies (sdAb) are increasing in popularity due to increased expression efficiency of functional binders and superior resistance to solvents. rAb-based immunochromatographic assays and surface plasmon resonance (SPR) biosensors have been reported to detect sub-regulatory levels of fungal (mycotoxins), marine (phycotoxins) and aquatic biotoxins in a wide range of food and environmental matrices, however this technology has yet to surpass the performances of the equivalent mAb- and pAb-based formats. As such the full potential of rAb technology in hapten biotoxin detection has yet to be achieved, but in time the inherent advantages of engineered rAb are set to provide the next generation of ultra-high performing binder reagents for the rapid and specific detection of hapten biotoxins.
authors.affiliation: Institute for Global Food Security (IGFS), School of Biological Sciences, Queen's University Belfast, Belfast, Northern Ireland, UK, o.kavanagh@qub.ac.uk.
authors.forename: Owen
authors.initials: O
authors.lastname: Kavanagh
authors.forename: Christopher T
authors.initials: CT
authors.lastname: Elliott
authors.forename: Katrina
authors.initials: K
authors.lastname: Campbell
mesh_terms: D000818:Animals; D000906:Antibodies / Q000235:genetics* / Q000276:immunology; D015374:Biosensing Techniques; D020650:Combinatorial Chemistry Techniques; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods; D005504:Food Analysis / Q000379:methods; D006241:Haptens / Q000276:immunology; D006801:Humans; D007118:Immunoassay / Q000379:methods; D007120:Immunochemistry / Q000379:methods*; D008970:Molecular Weight; D019151:Peptide Library; D011994:Recombinant Proteins / Q000235:genetics / Q000276:immunology*; D012680:Sensitivity and Specificity; D020349:Surface Plasmon Resonance; D014118:Toxins, Biological / Q000032:analysis / Q000276:immunology*
chemical_list: D000906:Antibodies; D006241:Haptens; D019151:Peptide Library; D011994:Recombinant Proteins; D014118:Toxins, Biological