Recombinant Alpaca Anti-RTA Single Domain Antibody (V1C7)

Figure 1 Neutralization capacity of V1C7 point mutants.

The two VHH point mutants at position 29 were compared against their parental VHHs in a Vero cell cytotoxicity assay. Ricin toxin-neutralizing activities associated with V1C7 versus V1C7 G29R.

Figure 2 Relative affinities of V1C7 (circles), V2B9 (squares), V2E8 (triangles), and V5C1 (inverted triangles) for ricin toxin, as determined by ELISA in which ricin was captured onto plastic surface by ASF.

Bazzoli, A., Vance, D. J., Rudolph, M. J., Rong, Y., Angalakurthi, S. K., Toth IV, R. T., ... & Mantis, N. J. (2017). Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies. Proteins: Structure, Function, and Bioinformatics, 85(11), 1994-2008.

Figure 3 Relationships between VHH binding affinities and toxin-neutralizing activities.

Each color represents a family; each dot represents an individual VHH within that family. The downward slope of the lines suggests a relationship between KD and TNA within a clonal family.

Vance, D. J., Tremblay, J. M., Rong, Y., Angalakurthi, S. K., Volkin, D. B., Middaugh, C. R., ... & Mantis, N. J. (2017). High-resolution epitope positioning of a large collection of neutralizing and nonneutralizing single-domain antibodies on the enzymatic and binding subunits of ricin toxin. Clin. Vaccine Immunol., 24(12), e00236-17.

Figure 4 4 Validation of cross-competition ELISA as a strategy for epitope localization on RTA.

V1C7 were subjected to competition ELISAs with a panel of RTA-specific MAbs representing neutralizing clusters I to IV.

Vance, D. J., Tremblay, J. M., Rong, Y., Angalakurthi, S. K., Volkin, D. B., Middaugh, C. R., ... & Mantis, N. J. (2017). High-resolution epitope positioning of a large collection of neutralizing and nonneutralizing single-domain antibodies on the enzymatic and binding subunits of ricin toxin. Clin. Vaccine Immunol., 24(12), e00236-17.