P. Lafaye et al., SIMILAR BINDING-PROPERTIES FOR A NEUTRALIZING ANTITETANUS TOXOID HUMAN MONOCLONAL-ANTIBODY AND ITS BACTERIALLY EXPRESSED FAB, Research in immunology, 146(6), 1995, pp. 373-382
A high-affinity anti-tenanus toroid (TT) human monoclonal antibody sho
wing neutralizing activity was isolated from a fusion between mouse my
eloma and human splenic cells. Fab fragments from this antibody were o
btained using a recombinant phage surface-display expression system. T
he parental antibody and the corresponding Fab had identical immunolog
ical activities, including specificity and affinity. These results con
firm the feasibility of developing Escherichia coli expression of mono
clonal human Fab from hybridoma cells.