Binding Affinity, Specificity and Comparative Biodistribution of the Parental Murine Monoclonal Antibody MX35 (Anti-NaPi2b) and Its Humanized Version Rebmab200.
Journal article, 2015

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.


Sture Lindegren

University of Gothenburg

Luciana N S Andrade

Tom Bäck

University of Gothenburg

Camila Maria L Machado

Bruno Brasil Horta

Carlos Buchpiguel

Ana Maria Moro

Oswaldo Keith Okamoto

Lars Jacobsson

University of Gothenburg

Elin Cederkrantz

University of Gothenburg

Kohshin Washiyama

University of Gothenburg

Emma Aneheim

University of Gothenburg

Stig Palm

University of Gothenburg

Holger Jensen

Maria Carolina B Tuma

Roger Chammas

Ragnar Hultborn

University of Gothenburg

Per Albertsson

University of Gothenburg


1932-6203 (ISSN) 19326203 (eISSN)

Vol. 10 5 e0126298-

Subject Categories

Radiology, Nuclear Medicine and Medical Imaging

Cancer and Oncology





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