Generation and Characterization of a Diabody Targeting the α v β 6 Integrin

Citations of this article
Mendeley users who have this article in their library.


The α v β 6 integrin is up-regulated in cancer and wound healing but it is not generally expressed in healthy adult tissue. There is increasing evidence that it has a role in cancer progression and will be a useful target for antibody-directed cancer therapies. We report a novel recombinant diabody antibody fragment that targets specifically α v β 6 and blocks its function. The diabody was engineered with a C-terminal hexahistidine tag (His tag), expressed in Pichia pastoris and purified by IMAC. Surface plasmon resonance (SPR) analysis of the purified diabody showed affinity in the nanomolar range. Pre-treatment of α v β 6 -expressing cells with the diabody resulted in a reduction of cell migration and adhesion to LAP, demonstrating biological function-blocking activity. After radio-labeling, using the His-tag for site-specific attachment of 99m Tc, the diabody retained affinity and targeted specifically to α v β 6 -expressing tumors in mice bearing isogenic α v β 6 +/- xenografts. Furthermore, the diabody was specifically internalized into α v β 6 -expressing cells, indicating warhead targeting potential. Our results indicate that the new α v β 6 diabody has a range of potential applications in imaging, function blocking or targeted delivery/internalization of therapeutic agents. © 2013 Kogelberg et al.




Kogelberg, H., Miranda, E., Burnet, J., Ellison, D., Tolner, B., Foster, J., … Chester, K. (2013). Generation and Characterization of a Diabody Targeting the α v β 6 Integrin. PLoS ONE, 8(9).

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free