PLoS ONE (Jan 2015)

Binding Affinity, Specificity and Comparative Biodistribution of the Parental Murine Monoclonal Antibody MX35 (Anti-NaPi2b) and Its Humanized Version Rebmab200.

  • Sture Lindegren,
  • Luciana N S Andrade,
  • Tom Bäck,
  • Camila Maria L Machado,
  • Bruno Brasil Horta,
  • Carlos Buchpiguel,
  • Ana Maria Moro,
  • Oswaldo Keith Okamoto,
  • Lars Jacobsson,
  • Elin Cederkrantz,
  • Kohshin Washiyama,
  • Emma Aneheim,
  • Stig Palm,
  • Holger Jensen,
  • Maria Carolina B Tuma,
  • Roger Chammas,
  • Ragnar Hultborn,
  • Per Albertsson

DOI
https://doi.org/10.1371/journal.pone.0126298
Journal volume & issue
Vol. 10, no. 5
p. e0126298

Abstract

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The aim of this preclinical study was to evaluate the characteristics of the monoclonal antibody Rebmab200, which is a humanized version of the ovarian-specific murine antibody MX35. This investigation contributes to the foundation for future clinical α-radioimmunotherapy of minimal residual ovarian cancer with 211At-Rebmab200. Here, the biodistribution of 211At-Rebmab200 was evaluated, as was the utility of 99mTc-Rebmab200 for bioimaging. Rebmab200 was directly compared with its murine counterpart MX35 in terms of its in-vitro capacity for binding the immobilized NaPi2B epitope and live cells; we also assessed its biodistribution in nude mice carrying subcutaneous OVCAR-3 tumors. Tumor antigen and cell binding were similar between Rebmab200 and murine MX35, as was biodistribution, including normal tissue uptake and in-vivo tumor binding. We also demonstrated that 99mTc-Rebmab200 can be used for single-photon emission computed tomography of subcutaneous ovarian carcinomas in tumor-bearing mice. Taken together, our data support the further development of Rebmab200 for radioimmunotherapy and diagnostics.